Biological Science (7th Edition)
7th Edition
ISBN: 9780134678320
Author: Scott Freeman, Kim Quillin, Lizabeth Allison, Michael Black, Greg Podgorski, Emily Taylor, Jeff Carmichael
Publisher: PEARSON
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Chapter 18, Problem 13PIAT
Summary Introduction
To review:
The gene regulatory circuit accounts for bacteria emitting light only when they reach a high cell density.
Introduction:
The light-producing genes are organized and operate under positive control. In molecular biology, positive regulation implies that a transcription factor is required to bind at the promoter site in gene to enhance RNA polymerase to initiate transcription. The activator that functions in this operon is LuxR. This activator is responsible for the emission of the light.
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Explain how adenyl cyclase enzymes function in signal transduction pathways.
Explain how kinase enzymes function in signal transduction pathways.
The diagram below shows a closeup of regulatory proteins binding to one of the UASG elements near the GAL7, GALI0, and GALI
genes, which code for the protein products needed for yeast to use the sugar galactose. The red triangle symbolizes an "effector"
molecule that binds to Gal80p. In this hypothesis (which has since been shown to be incorrect), what could be happening to Gal80p
when it is bound to the effector molecule that causes it to change its position and uncover the Gal4p transcriptional activation domain.
Hint: think about what effector molecules do upon binding to proteins such as the the Lac repressor protein or the CAP protein.
Galactose absent, glucose absent
Gal80p.
_Activation domain
Gal4p
dimer
-Binding domain
UASG
Galactose present, glucose absent
Activation domain
Gal80p-
Binding domain
UASG
For the toolbar, press ALT+F10 (PC) or ALT+FN+F10 (Mac).
The output of RTK pathways is often the activation of MAP Kinase. Explain how MAPK
can lead to activation of a specific subset of proteins, leading to distinct effects in different
cell types in response to the same growth signal.
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- See figure 12.16b regarding the process by which cyclin regulates the Cdk. Suppose that the cyclin binding site in the Cdk contains these FOUR amino acids in this order from top to bottom: serine, lysine, aspartic acid acid and lysine and the Cdk binding site in the cyclin contains these FOUR amino acids in this order from top to bottom: aspartic acid, aspartic acid, lysine and serine. Use the schematics below to show the R groups and how they might interact to create the cyclin.cdk complex. Label both binding sites, show all charges that will be used to create any bonds, and label all bonds formed and add the ATP active site. Cyclin Serine Lysine Aspartic "Acid Lysine -OH NH3t -Coo NH3+ NH3 + -OH Aspartic Aad Aspartic Acid /Lysine Serine сокarrow_forwardThe figure below details a pathway in yeast involving kinases and a phosphatase and the regulation of a specific cyclin-cdk complex. CAK kinase controls the phosphorylation of Thr161. The phosphorylation of Tyr15 is controlled by Wee1 and Cdc25. In this problem, focus on the phosphorylation of Tyr15 by Wee1 and Cdc25. 1. If Wee1 kinase was inactive, what would happen to the cyclin-cdc2 complex? Would the cells enter mitosis and divide more or less often? Would the cells end up being smaller or larger than normal? 2. If Cdc25 phosphatase was inactive, what would happen to the cyclin-cdc2 complex? Would the cells enter mitosis and divide more or less often? Would the cells end up being smaller or larger than normal?arrow_forwardUse the SGF-signaling pathway image as a reference, to answer the following questions. Use the data provided to EXPLAIN if the cell will get to the response step or not. Keep in mind the purpose of this pathway is to cause skin cell division Growth Factor (GF-signal) Activation of GF Receptor (RTK-receptor) To cause Cell proliferation/cell division (Response) Plasma membrane Sos Grb2 (Ras GEF) (adapter) Raf МАРКK Mek МАРКK Activation of target genes that stimulate proliferation Erk МАРК You have a skin cell in a dish and have added Neural Growth Factor (NGF) to the cell media (the liquid the cell needs to live).arrow_forward
- Now read this abstract from a 2013 journal article What is the authors' explanation of how Gal80p works? Note UASG from the question above is the same as UASGAL The DNA-binding transcriptional activator Gal4 and its regulators Gal80 and Gal3 constitute a galactose-responsive switch for the GAL genes of Saccharomyces cerevisiae. Gal4 binds to GAL gene UASGAL. (upstream activation sequence in GAL gene pro- moter) sites as a dimer via its N-terminal domain and activates transcription via a C-terminal transcription activation domain (AD). In the absence of galactose, a Gal80 dimer binds to a dimer of Gal4, masking the Gal4AD. Galactose triggers Gal3-Gal80 interaction to rapidly initiate Gal4-mediated transcription activation. Just how Gal3 alters Gal80 to relieve Gals0 inhibition of Gal4 has been unknown, but previous analyses of Gal80 mutants suggested a possible competition between Gal3-Gal80 and Gal80 self-association interactions. Here we assayed Gal80-Gal80 interactions and tested for…arrow_forwardCancers are often caused by overactive growth factor receptor signaling (remember growth factor receptors are enzyme-linked receptor pathways). If you were able to use gene therapy to overexpress a particular protein in a cancer cell, which of the following might be useful to overexpress in order to combatt cancer? a GAP that acts on Ras a phosphatase that acts on GPCR a protein that enhances the activity of Akt a ubiqtuin ligase that acts on the MAPK phophatasearrow_forwardThe exchange of materials between RPE cells and the rods and cone cells is very important. Suggest by which membrane transport methods ions, proteins and damaged fragments of rod cells would be taken into the RPE cells. Outline the properties of stem cells which will help to repair the RPE layer of a patients retina after implantation of the thin sheet of cells. Outline how the presence of a base substitution mutation in the ABCA4 gene would result in the synthesis of a protein which cannot carry out its normal function. Need short answer in text solution and ASAP .arrow_forward
- You have isolated a new species of infectious bacteria. The bacterium releases a toxin that you believe is adversely affecting heterotrimeric Gs (stimulatory)-protein-based signaling. To explore this hypothesis you use an epithelial cell line that is expressing a cyan fluorescent protein (CFP)-labeled α subunit and a yellow fluorescent protein (YFP)-labeled β subunit of a heterotrimeric Gs-protein. CFP emits blue light and has excitation and emission wavelengths of 440 nm and 490 nm, respectively. YFP emits yellow light and has excitation and emission wavelengths of 490 nm and 527 nm, respectively. To test your hypothesis, you perform two experiments. First, you apply a signaling ligand known to activate this Gs protein and track yellow fluorescence. Second, you apply the signaling ligand and the purified bacterial toxin simultaneously and track yellow fluorescence. Which of the following conclusion will you draw based on the above experimental data? The toxin locks the α subunit…arrow_forwardA -------| B-------> Violet A linear switch-regulation pathway of the type shown here controls flower color in a certain species. The wildtype color is violet, but mutants can be either white or purple. Gene products A and B act in the pathway at the positions and in the manner shown (A is inhibitory, B is intensifying). A and B are the products of genes A and B, respectively. What are the expected phenotypes of: (a) A loss-of-function mutation in A? (b) A gain-of-function mutation in A? (c) A loss-of-function mutation in B? (d) A gain-of-function mutation in B?arrow_forwardWe have studied Ras signal transduction pathway. In an experiment, two different mutations were produced using different chemicals. The proteins with mutation are listed below. State what will be the effect of each mutation and explain whether it will result in cell proliferation or not. GEF protein GTPasearrow_forward
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