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Seventeenth week (10/16/2008)

We made a ligation reaction.
prepare two tubes, one with H2O, Buffer, vector, insert and ligase, and the other the same but without the insert, this will serve to verify that the two ends of the vector are not back together. We leave in a water bath at 26 ° C for one hour to correctly insert is linked to the vector. We then proceeded with the following protocol: Transformation of E.
coli
1. Add 100 ml of competent cells and 20 ml of ligation rx a sterile Eppendorf. Make control with 100 ml of competent cells and 0.5 ml of control plasmid (Qiagen kit purified x)
2. Incubate 30 minutes on ice
3. Incubate 2 minutes to 42 ˚ C
4. Incubate 5 min on ice
5. Add 1 ml (or 450 ml) of LB medium without ampicillin
6. Incubate 1 hour at 37 ˚ C to 225 rpm
7. Centrifuge cells and resuspend the pellet in remaining supernatant
8. Sowing the entire contents of each tube on plates with LB medium + AmpicilinaColocar in oven at 37 ˚ C

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Sixteenth week (02/10/2008)

We PCR to amplify the insert (800 bp promoter UGA3), and cut with restruccion enzymes (EcoRI and Bami .) When we add vector tube and let phosphatase in oven at 37 º C for an hour and a half to be desfosfate well. After three buffers purify the vector and insert.
prepare an agarose gel where we put the inserts and let it run.

We

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Fifteenth week (09/25/2008)

transformations again two weeks ago, as some had fungal or other contamination.
done likewise;
strains grew on rich medium plates, clean, centrifuged, use a solution that helps the plasmid into the cell, incubated and plated .

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Fourteenth week (18/09/2008)

note the results of the previous week. We used the plasmid
to purify one of the weeks and cut with a restriction enzyme ( HindIII .) We did it twice.
This is called digestion of a plasmid . It uses a buffer specific enzymes, the plasmid and filled with water. Then placed at 37 ° C during the period of one hour and a half.
In agarose gel 8% m / v ran the undigested plasmid at different concentrations and the two plasmids also digested in different concentrations.

The image shown in the first two wells the undigested plasmids (the two bands observed belong to the two ways in which this CCC (predominant) and OC (one of the chains broke leaving plasmid in a relaxed state). The following wells show the once digested plasmid at different concentrations, where you see a band that belongs to the state of linear plasmid (cut the two strings). At the end is the marker and use it to measure the amount of base pairs so make sure everything ran correctly.

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Thirteenth week (04/09/2008)

Today transformed cells to introduce plasmids inside. In this case the cells were transformed Ura - and thus can not grow in media without uracil . He plasmid introduce them given the ura gene 3 with the ability to generate their own uracil therefore join those who will survive in the uracil -.
To accomplish all this:
-strains grew on rich medium plates
- cells resuspended in 1 ml of sterile water and centrifuged
-discard the supernatant and resuspended in the liquid remaining
-added a solution that helps the plasmid enter the cell (in addition to hitshock the next step) the
-cell suspension spent 20 microL another eppendorf and added the plasmid DNA
-the incubate 30 minutes at 42 °
-added 1 ml sterile water, centrifuged to lower-and
cells plated in the middle

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Introduction

elucidate the molecular events triggered in response to changes in nutrient availability, analyzing gene regulation processes in model organism Saccharomyces cerevisiae

Any cell

different types of nutrients needed for growth. Cells are able to sense changes in nutrient growth medium and adapt to them. Thus, the processes that mediate various cellular responses occur sequentially and are: reception, transduction and response. The reception involves the sensing of different nutrients and proteins in the plasma membrane of cells. Transduction is the mechanism by which signals are sent or within cells generate a cellular response, which may be the activation of enzymes of a particular metabolic pathway and / or activate the transcription of specific genes. Each cell
has within it a nucleus that contains, among other things, the information (DNA) to enable it to function properly. This information in turn, is divided into small segments, in packages that are called genes. Each gene, after being transcribed and translated, produces a special protein, ie each gene has enough information to synthesize a protein.

As experimental model, cells will be used yeast Saccharomyces cerevisiae is a unicellular eukaryotic organism non-pathogenic, easy handling, rapid growth in defined culture media and whose complete genome sequence is known. Taking into account the evolutionary conservation of the signaling pathways triggered in response to nutrient medium, the use of S. cerevisiae as a model for the study of signal transduction will clarify the major challenge is to understand how signals produced by nutrients present in the extracellular environment are integrated and coordinated by the cells.

In this picture you can see a yeast cell gemando (reproducing asexually).

can also observe the nucleus and vacuole.

In the laboratory studying the regulation of gene UGA4, which is an excellent model for studying gene response to changes in the extracellular environment and is subject to complex regulation and also some of the key proteins involved in this regulation are conserved from yeast to man. This is the case, for example, transcription factors GATA family, many of which are important in regulating UGA4, and also the Tor1 protein, kinase that has a central role in controlling growth response to nutrient availability in both flies and yeast as cells mamíferos1, 2.
UGA4 is the gene that codes for Uga4 protein. This protein is a permease located in the plasma membrane and allows the incorporation of d-aminolevúlico acid (ALA) 3.4 and y-aminobutyric acid (GABA) 5.6.

ALA has no biological function that is essential for the cell, is incorporated by this because of its structure , which is similar to that of GABA.
GABA can be used by the yeast cells as a source of nitrogen, but is a poor source in compared to rich sources of nitrogen and ammonia. Factors influencing the suppression or induction of gene expression, depending on the situation in which the cell is located. The gene to be expressed only in the absence of a source of nitrogen (as ammonium) in the absence of such a source, the cell triggers mechanisms to survive in such conditions. In the promoter sequence of the gene UGA4 two important sites known as GABA and UAS-UAS-GATA. In each of these factors influence the sticking repress or induce its expression. UGA4 gene expression depends on the presence of an inducer, GABA5, 7. Induction requires the action of two factors transcription, a specific Uga3 and other pleiotropic, Uga35, which act through activating sequence rich in GC nucleotides (UASGABA) 8.9. The UGA4 gene regulatory region also contains four adjacent repeats heptanucleótido 5'-CGAT (A / T) AG-3 'which is an UASGATA. On the latter acting GATA factors can act as positive and negative factors. The negative (and Gzf3 Uga43) compete with the positive (Gln3 and GAT1) and that "wins" sticks to the gene promoter. When there is a rich source of nitrogen, the cell does not waste energy synthesizing proteins carrying GABA8, 10.11, positive factors. Gln3 and GAT1, was found in the cytoplasm bound to the protein Ure2 from acting on the UAS-GATA element, and therefore, the negative factors "win", which leads to repression of the expression of UGA4. In this case the negative factors bind to the UAS-GATA site.

When there is a rich source but there are GABA in the medium, the cell adapts to change and active all the machinery to synthesize the protein Uga4, in other words, GABA induces gene expression UGA45, 7.9 . Positive factors dissociate from Ure2 and translocate to the nucleus where they move to the negative factors binding to the promoter and allowing expression gen9, 12. The interaction between the positive factors with GAT1 Gln3 and Ure2 is modulated by the phosphorylation status of these factors which in turn depends on the kinase activity Tor13-15.
The main objective of this internship is to familiarize with different molecular biology techniques through participation in a project that studies the signaling cascade that leads to the regulation of gene expression UGA4 by extracellular amino acids. Molecular mechanisms signaling cascade that is not fully understood but it is known that the SPS sensor complex is involved.
This complex is known as SPS16-18 for its three protein components (Ssy1p, Ptr3p and Ssy5p) and activated after the sensing of extracellular amino acids and possibly intracelulares19. Ssy1 is a membrane protein that resembles an amino acid permease but functions only as a sensor. Ssy5 ptr3 and interact with Ssy1 form a dynamic protein complex. It has been determined a large number of genes regulated by the activity of this sensor and many of these genes encode proteins involved in amino acid transport. Among them, AGP1 BAP2 and respond to amino acids via the SPS through Stp1 transcription factors, and Uga3520 STP2.

Stp1 and STP2 factors act in response to extracellular amino acid sensing on UASA elements present in promoters of permeases, such as BAP2 and BAP3. Importantly, the large sequence similarity between elements and UASGABA21 UASA, 22. STP2 Stp1 and are synthesized as latent factors and remain trapped in the cytoplasm through the amino terminal regulatory domain. Also three proteins in the inner nuclear membrane, ASI1, Asi3 ASI2 and participate in retaining and STP2 Stp1 latent in citoplasma23, 24. In response to amino acids, active Ssy1 Ssy5 protease that in turn cleaves the regulatory domain and STP2 Stp1, leading to activation of these factors. Their processed forms are transported to the nucleus where genes regulated transactivator SPS20 ,25-27.


Bibliografía:
1. De Virgilio, C. & Loewith, R. Cell growth control: little eukaryotes make big contributions. Oncogene 25, 6392-415 (2006).
2. Beck, T. & Hall, M. N. The TOR signalling pathway controls nuclear localization of nutrient-regulated transcription factors. Nature 402, 689-92 (1999).
3. Bermudez Moretti, M., Correa Garcia, S., Stella, C., Ramos, E. & Batlle, A. M. Delta-aminolevulinic acid transport in Saccharomyces cerevisiae. Int J Biochem 25, 1917-24 (1993).
4. Bermudez Moretti, M., Correa Garcia, S., Ramos, E. & Batlle, A. delta-Aminolevulinic acid uptake is mediated by the gamma-aminobutyric acid-specific permease UGA4. Cell Mol Biol (Noisy-le-grand) 42, 519-23 (1996).
5. Andre, B., Hein, C., Grenson, M. & Jauniaux, J. C. Cloning and expression of the UGA4 gene coding for the inducible GABA-specific transport protein of Saccharomyces cerevisiae. Mol Gen Genet 237, 17-25 (1993).
6. Uemura, T., Tomonari, Y., Kashiwagi, K. & Igarashi, K. Uptake of GABA and putrescine by UGA4 on the vacuolar membrane in Saccharomyces cerevisiae. Biochem Biophys Res Commun 315, 1082-7 (2004).
7. Andre, B. The UGA3 gene regulating the GABA catabolic pathway in Saccharomyces cerevisiae codes for a putative zinc-finger protein acting on RNA amount. Mol Gen Genet 220, 269-76 (1990).
8. Andre, B. et al. Two mutually exclusive regulatory systems inhibit UASGATA, a cluster of 5'-GAT(A/T)A-3' upstream from the UGA4 gene of Saccharomyces cerevisiae. Nucleic Acids Res 23, 558-64 (1995).
9. Talibi, D., Grenson, M. & Andre, B. Cis- and trans-acting elements determining induction of the genes of the gamma-aminobutyrate (GABA) utilization pathway in Saccharomyces cerevisiae. Nucleic Acids Res 23, 550-7 (1995).
10. Vissers, S., Andre, B., Muyldermans, F. & Grenson, M. Positive and negative regulatory elements control the expression of the UGA4 gene coding for the inducible 4-aminobutyric-acid-specific permease in Saccharomyces cerevisiae. Eur J Biochem 181, 357-61 (1989).
11. Grenson, M. 4-Aminobutyric acid (GABA) uptake in Baker's yeast Saccharomyces cerevisiae is mediated by the general amino acid permease, the proline permease and a GABA specific permease integrated into the GABA-catabolic pathway. Life Sci Adv Biochem 6, 35-39 (1987).
12. Idicula, A. M., Blatch, G. L., Cooper, T. G. & Dorrington, R. A. Binding and activation by the zinc cluster transcription factors of Saccharomyces cerevisiae. Redefining the UASGABA and its interaction with Uga3p. J Biol Chem 277, 45977-83 (2002).
13. Magasanik, B. & Kaiser, C. A. Nitrogen regulation in Saccharomyces cerevisiae. Gene 290, 1-18 (2002).
14. Kulkarni, A., Buford, T. D., Rai, R. & Cooper, T. G. Differing responses of Gat1 and Gln3 phosphorylation and localization to rapamycin and methionine sulfoximine treatment in Saccharomyces cerevisiae. FEMS Yeast Res 6, 218-29 (2006).
15. Bermudez Moretti, M. et al. Evidence that 4-aminobutyric acid and 5-aminolevulinic acid share a common transport system into Saccharomyces cerevisiae. Int J Biochem Cell Biol 27, 169-73 (1995).
16. Didion, T., Regenberg, B., Jorgensen, M. U., Kielland-Brandt, M. C. & Andersen, H. A. The permease homologue Ssy1p controls the expression of amino acid and peptide transporter genes in Saccharomyces cerevisiae. Mol Microbiol 27, 643-50 (1998).
17. Iraqui, I. et al. Amino acid signaling in Saccharomyces cerevisiae: a permease-like sensor of external amino acids and F-Box protein Grr1p are required for transcriptional induction of the AGP1 gene, which encodes a broad-specificity amino acid permease. Mol Cell Biol 19, 989-1001 (1999).
18. Klasson, H., Fink, G. R. & Ljungdahl, P. O. Ssy1p and Ptr3p are plasma membrane components of a yeast system that senses extracellular amino acids. Mol Cell Biol 19, 5405-16 (1999).
19. Wu, B. et al. Competitive intra- and extracellular nutrient sensing by the transporter homologue Ssy1p. J Cell Biol 173, 327-31 (2006).
20. Abdel-Sater, F., Iraqui, I., Urrestarazu, A. & Andre, B. The external amino acid signaling pathway promotes activation of Stp1 and Uga35/Dal81 transcription factors for induction of the AGP1 gene in Saccharomyces cerevisiae. Genetics 166, 1727-39 (2004).
21. de Boer, M. et al. Stp1p, Stp2p and Abf1p are involved in regulation of expression of the amino acid transporter gene BAP3 of Saccharomyces cerevisiae. Nucleic Acids Res 28, 974-81 (2000).
22. Nielsen, P. S. et al. Transcriptional regulation of the Saccharomyces cerevisiae amino acid permease gene BAP2. Mol Gen Genet 264, 613-22 (2001).
23. Boban, M. & Ljungdahl, P. O. Dal81 enhances Stp1- and Stp2-dependent transcription necessitating negative modulation by inner nuclear membrane protein Asi1 in Saccharomyces cerevisiae. Genetics 176, 2087-97 (2007).
24. Boban, M. et al. Asi1 is an inner nuclear membrane protein that restricts promoter access of two latent transcription factors. J Cell Biol 173, 695-707 (2006).
25. Abdel-Sater, F., El Bakkoury, M., Urrestarazu, A., Vissers, S. & Andre, B. Amino acid signaling in yeast: casein kinase I and the Ssy5 endoprotease are key determinants of endoproteolytic activation of the membrane-bound Stp1 transcription factor. Mol Cell Biol 24, 9771-85 (2004).
26. Andreasson, C., Heessen, S. & Ljungdahl, P. O. Regulation of transcription factor latency by receptor-activated proteolysis. Genes Dev 20, 1563-8 (2006).
27. Andreasson, C. & Ljungdahl, P. O. The N-terminal regulatory domain of Stp1p is modular and, fused to an artificial transcription factor, confers full Ssy1p-Ptr3p-Ssy5p sensor control. Mol Cell Biol 24, 7503-13 (2004).

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Twelfth week (14/08/2008)

still working in the Introduction.

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Eleventh week (07/24/1908) Tenth

began with the introduction of labor.
We asked our questions to Sabrina, she gave us papers, we explain other issues and gave us more information.

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week (07/17/2008)

Growth prepare three media: LB

Middle (for growing bacteria):
· Extract 0.5% yeast
·
· NaCl 1% 1% Peptone Agar 2%
·

YPD medium (rich medium to grow yeast)
• And (yeast extract) 1%
· P (peptone) 2%
· D (dextrose / glucose) 2% 2% Agar
·

Middle YNB-DO (URA minimal medium (-) to grow yeast)
· YNB (yeast nitrogen base) 0.67%
· Glucose 2% Drop out
· URA (-) 0.19% Agar 2.5%
·

All agar media were added because we do plates.
Autoclaving the media along with tips and Erlenmeyer flasks to sterilize.
prepare 15 plates with media, 5 plates for each and labeled.
prepare a buffer that was needed in the laboratory, Z buffer used, inter alia, for the testing of B-gal two weeks ago. We weighed
components as we did with media, but without autoclaving. Susana
explained as primers are constructed and gave us a problem to do.

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Ninth week (10/07/2008)

We found what we were wrong last time, and after going back to Excel all we realized that the mistake he had was some brackets in the equations to get Miller units.

With the corrected data, we figure in a special program and found that it was actually correct as is the experience.

Sabrina gave us a method protocol Chip (chromatin immunoprecitation) in English, to familiarize with the vocabulary and be able to deduce and understand what each step was and what was required.
This technique consists basically of:
· Fix or leave everything static (covalently joining if any, binding to the protein) using formaldehyde
§ comparing sonicated to break DNA into smaller fragments
· is added to a protein that helps clean up the proteins that are more
· is puts an antibody that attaches to the protein that interests me
§ comparing add a ball of protein that is also attached to the antibody and this precipitated PCR
· is made and analyzes the content.

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Eighth week (07/03/1908 )

reporter gene assay, using the method of Miller, we found the activity of the b-galactosidase.
substrate was added to samples containing other compounds to see if these interfere with the activity of the enzyme, the product that gives this reaction with ONPG is yellow and is measured in a spectrophotometer. We
aliquot tubes last week and we add Buffer Z. SDS and chloroform to put that then to put ONPG, this substance can come, adding that, the b-galactosidase to catalyze the reaction starts and when the product (the yellow) it stops with Na2CO3 and placed in cold. (We duplicate samples and every 30 seconds to add ONPG tubes). We note
initial time and final time of the reaction. We take the cell density of the surplus ml tubes at an absorbance at 570 nm. Absorbance for Miller units at 420 nm. Make a table that includes all values \u200b\u200band also a chart appears in Miller units versus time.

While we thought we had worked well and the absorbance were quite successful in the time to make the graphics got very poorly and a straight illogical.

Figure if we had done well would have been something like

We

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seventh week (26/06/08)

induction.
Day 1: take a colony of yeast containing a plasmid (YEP -357) and placed on minimal medium, leave it overnight.
Day 2: it is a dilution of the medium and leaving it overnight.
Day 3: the medium is divided into three tubes are centrifuged pellet staying with and adding back the minimal media but cool (one of the three tubes were added Leucine (un aminoácido )). Después de 30 minutos al tubo de los aminoácidos y a otro se le agrega GABA .
Se toma una muestra a tiempo 0 de los tres tubos y otras a los 120 minutos.
El objetivo es saber en que condiciones el gen se induce mejor, si afecta la presencia de aminoácidos en la inducción y como se ven estos cambios según la variación del tiempo.

Sabrina también nos explicó como hacer para saber si una proteína interactúa con el gen UGA 4. para eso se usa formaldehido que une covalentemente a la proteína con el gen. Después un antibody and agarose ball bind with the protein. This is precipitated using the centrifuge.
After that you can have 2 possibilities: that the protein sticks to UGA 4 and rush with this, or stick to something else and is the UGA gene 4 in the supernatant . If UGA is
4 in the supernatant means that the protein does not interact with it.
was verified by PCR

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Week Six (19/06/2008)

With an agarose gel ran the 4 colonies that were mutated so as to confirm the mutation of the colonies planted earlier. And given that 3 colonies were mutated and a given mixture of cells. This was done by using 2 primers that allow to know which mutated through the gel. Sabrina
After we explained what we were going to do next week.

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Week Five (12/06/08)

We check each cell mutations by a PCR and running on agarose gel , we obtained positive product with primers used for mutant colonies and some other mixture of cells, so seeded in a petri plates for more colonies and to confirm a mutation. The mutation is done by homologous recombination with a fragment of DNA containing a selectable marker URA 3. Then with specific primers for cells type wild and mutant cells I can see if there is mutation.

Ampicillin sterilize by filtering technique in a laminar flow and placing tubes in 20 to save and not to deteriorate the pregnant thawing and freezing all the time. The ampicillin comes in 1000x concentration (0.1 g / ml).

prepare a growth medium with:
1% yeast extract 2% peptone

2% Glucose Agar
2% (to prepare plates).

The image is of PCR and plasmid last week.
in the first well is the marker and through the well of the PCR first the positive and then negative (as there is nothing we can say that there was no contamination), and the last is that of the plasmid .
the person selling the marker delivery also with a paper showing how it will run and the bands that show sizes as base pairs. So we know how many base pairs have the PCR and plasmid .

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Fourth week (06/05/2008)

plasmids extracted from the bacteria E. Coli of our environment LB, precisely following the proper protocol steps: We

an aliquot of 5 ml of our culture of bacteria E. Coli and centrifuged, leaving us with the pellet (the supernatant is composed of medium components and the pellet are bacteria) added a
Buffer has EDTA (by chelating action helps to further destabilize the bacterial membrane) also has a blue dye, Lyse Blue, (which tells me when everything is homogenized). Add another solution
Buffer (comprising NaOH and SDS ). There is a basic analysis, and color change from clear to blue. Be mixed by immersion, because everything I have inside of the tube is too sensitive, until the blue color is the same everywhere. We added the third
buffer which lowers the pH favoring renaturation of DNA . but, as an abrupt change is renature wrong and what I get is a whole precipitate membrane debris, walls genomic DNA etc., the dye changes from blue to colorless (dip mix again.) As the plasmid
is very small and it is linked physically , not separated and can renature well. I have left in solution.
centrifuged.
We put the solution in a tall column where you will be united in the Recina DNA, passing through it (enzymes, etc). Centrifuge.
We wash with Buffer separating proteins and salts plasmid. Centrifuge. He adds another
Buffer to continue washing and purifying our plasmid. Centrifuged. Buffer place another that will take off the plasmid the tall column (centrifuging to ensure that under all purified plasmid).

prepare an agarose gel 1% w / v in 45 ml
placed in the wells of the gel three PCR and plasmid solution (each with 1.25 ul of loading buffer (which by its density, contains glycerin, helps us do what we sow sow down to posillo and not left floating, and the dye that is allows us to see the front fluently).

Next week we will see the results of another agarose gel .

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Third week (29/05/2008 )

amplified DNA sequence of 800 bp promoter UGA -3. For this we use the PCR technique , components to accomplish this are:
Buffer dNTP

MgCl 2 First

DNA pol ( Taq polymerase , thermostable , survive high temperatures)
mold genomic DNA

H2O concentrations calculated to ensure that all of this in 150 ul

* A mix when everything is important to note that the first thing you should put the water and the B uffer because other components are very sensitive to place in the vacuum tube and nothing happens to them.

prepare three tubes with 50 ul PCR each mixture. Two of them with the mold (we will call positive (+)) and one without it (let's call this negative (-)). Tube is necessary to negative because it indicates whether there was contamination or not and whether what I have in the tubes is only gene DNA gel UGA also -3 or more. We want to ensure only be amplifying the selected sequence.

To make PCR is a program where everything is heated to 94 ° C (to separate DNA chains ) lowering the temperature to 63 ° C (at this temperature are joined primers) and then rises to 72 ° C (the temperature optimum for polymerization ). This program is done in cycles amplify and have a lot of product.

Program used: 94 ° C 5

min 94 ° C 1 min \\
63 ° C 1 min ) is repeated 30 times.
72 ° C 2 min /
72 ° C 5 min

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Second week (22/05/08)

sow bacteria E. Coli with a plasmid into, to massively multiply their numbers and so have many plasmids can then use for cloning.

To achieve this we had to do the following:

prepare the LB growth medium (NaCl 1%, yeast extract 0.5% Peptone 1%), to weigh the components we use an analytical balance and then with a test tube, add 100 ml of distilled water. Labeled and sent to be sterilized (30 minutes) with about three Erlenmeyer flasks. Put the medium in the Erlenmeyer flasks and add 10 ul of 100mg/ml ampicillin (1000x) with a micropipette.

Then sow the bacterium E. Coli (strain DHSα) with plasmids (YEP-357). We put the Erlenmeyer flasks in an incubator at 37 ° C (shaker).

We used this strain of E. coli because we want to do is to differentiate the bacteria with the plasmid of which do not have and this is achieved with this strain, which is sensitive to ampicillin. Plasmid achieves the bacteria that has built not die and do not have it together. We use this plasmid
because it can replicate in yeast and bacteria and also has a reporter gene (β-galactose).

* The image is plasmid-357 Yep.

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first week (05/15/2008)

Upon arrival at the laboratory after an exhaustive search by the university, we expect the researcher Susana Correa García. As she explained to us what it is about the internship, some theoretical data and what we had planned to be added also to the assistant Sabrina Cardillo talk with which we work most time.
Then at 10 am we left to attend an informative lecture was provided by the UBA. This consisted of two videos and explained and appointed safety standards and that one should work and what to do in emergencies.
After the talk returned to the laboratory and followed us alone Sabrina instructed on theoretical content, explained the deeper themes and techniques that we would use appointed during the internship (PCR), showed us how some teams and some materials. We also sent information on the subject via the Internet.

Some topics we discussed:
Bacteria: E.
Coli Gene: Saccharomyces cerevisiae UGA4 Technical
cloned: PCR

Ivan and Victoria

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Chemistry Project Human Genome ORT

Research in Biochemistry and Molecular Proteomics 2008

For the fourth year students in the last year of the specialty chemical ORT Technical School (Argentina) made their final projects at various universities and research centers with recognized professionals. The working methodology avoids the didactic transposition allowing students to make their final activity where knowledge is being generated.

The relationship between the average level toward degree is sponsored by the CONICET (National Council for Scientific and Technical Research.

research projects for the current year are:

1. Expression Evaluation adhesion molecule epithelial cadherin in human normal and tumor tissues.
Investigator: Dr. Monica Vazquez-Levin.
Institute: Institute of Molecular Biology and Medicine (IBYME - CONICET).
Students: Yael Dobzewicz Y Gala Szapiro.
Link: http://www.proyecto-6q.blogspot.com/

2. Action hexachlorobenzene (HCB) on uroporphyrinogen a human hepatocyte cell line. Mechanism of action.
Researcher: Dr. Maria del Carmen Ríos de Molina.
Institute: Biological Chemistry Department, Faculty of Natural Sciences.
Students: Lucas Toiw and Uriel Frid.
Link: http://www.proyectofrid-toiw08.blogspot.com/

3. Experimental models of metabolic diseases: porphyria and Metabolic Syndrome. Proteomics and Metabolomics of these disturbances.
Investigator: Dr. Marta White Mazzetti.
Institute: Biological Chemistry Department, Faculty of Natural Sciences (UBA).
Students: Maria Duperron and Mauro Elencwajg.
Link: http://proyectofinal6q.blogspot.com/

4. Hemodynamic Factors not related to the genesis and evolution of proteinuria in progressive renal disease.
Investigator: Dr. Elsa Zotta.
Institute: physiopathology Laboratory, Department of Physiology, Faculty of Medicine, UBA.

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Hi, we are Ivan and Victoria.
This is the blog of our final project, specialty chemistry.

Our internship cover:

The study of the molecular mechanisms involved in regulating gene of Saccharomyces cervisiae UGA4 in response to changes in nutrient availability to elucidate the different signaling cascades triggered by these nutrients and to establish their interconnections.

Researcher: Dr Susana Correa García.