Becker's World of the Cell (9th Edition)
Becker's World of the Cell (9th Edition)
9th Edition
ISBN: 9780321934925
Author: Jeff Hardin, Gregory Paul Bertoni
Publisher: PEARSON
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Chapter 20, Problem 20.13PS

Levels of Control. If sea urchin zygotes are exposed to actinomycin D, an inhibitor of RNA synthesis, during the early stages of embryonic development, protein synthesis and development continue until the embryos form a hollow ball of cells, or blastula, with hundreds of cells. However, if the same inhibitor is added later during embryonic development, protein synthesis is severely depressed, and normal embryonic development halts. How might you explain these observations?

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Please help me with this question. More than one answer may be correct. THe graph relating to the information is included below. The figure shows the number of cells that have clusters of IRE1 molecules after those cells are treated with various levels of thapsigargin (Tg), a chemical that can induce ER stress. IRE1 can form these clusters when ER stress is induced and this clustering can cause activation of RNAse activity in IRE1. In this experiment, normal IRE1 was used (IRE1α) that can bind to Sec61, along with a modified version of IRE1 that binds to Sec61 more weakly than normal IRE1 (wIRE1α), and another modified version that binds to Sec61 more strongly than normal IRE1 (sIRE1α). From this figure you can conclude that: Question 18 options: IRE1 binding to Sec61 promotes the formation of IRE1 clumps IRE1 binding to Sec61 prevents the formation of IRE1 clumps co-translational translocation is a key process the golgi aparatus is heavily involved in the unfolded protein response The…
Inducers and Inhibitors of AEP. Short peptides such as legumain stabilization and activity modulation (LSAM) domain and αvβ3 integrin could enhance the activity of AEP. LSAM domain known as the prodomain of AEP blocks substrate binding before activation. This prodomain has a helical structure and two independent peptides. One is an activation peptide (AP, K287 to N323), and the other is a LSAM domain. LSAM domain remains even after AP is cleaved and released from protease at neutral pH via electrostatic interaction. AEP without LSAM domain has a lower melting temperature than AEP with LSAM domain [77, 117]. Another short peptide, αvβ3 integrin, can directly interact with AEP, and after forming a complex, the optimal pH for AEP activity is increased from 5.5 to 6.0. It indicates that αvβ3 binding could induce conformational stabilization of AEP accompanied by deprotonated C189. αvβ3 does not directly interact with the AEP active site; however, AEP docks to the αvβ3 RGD-binding site…
TPA protein function. Use at least two sentences to describe the function of the TPA protein.
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