BIOLOGY
BIOLOGY
5th Edition
ISBN: 9781264104680
Author: BROOKER
Publisher: MCG
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Chapter 4, Problem 9TY
Summary Introduction

Introduction: Every organelle present in a cell performs a specific function. Short amino acid sequences, responsible for directing proteins to their locations, are known as sorting signals. A specific cellular component recognizes its corresponding sorting signal and the protein carrying that signal is redirected to its correct location.

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Indicate (x) if the following statements about synthesis of proteins containing an ER signal sequence are True or False: True False i. Translation is initiated by ribosomes located on the ER membrane The signal recognition particle (SRP) binds a sequence of nonpolar (hydrophobic) amino acids. ii. iii. The ER signal sequence may be cleaved by signal peptidase on the cytoplasmic side of the ER membrane. iv. The part of a transmembrane protein that will ultimately be located outside of the cell is inserted into the lumen of the ER during translation. A stop transfer sequence is a series of polar amino acids that halts translocation of a newly synthesized peptide into the ER lumen.
In eukaryotic cells, secreted proteins are initially directed to the endoplasmic reticulum and then via the Golgi, where they are released into the extracellular environment through secretory vesicles. A more easier way would be for secretory protein-producing ribosomes to be localised to a translocon in the plasma membrane, with the protein being secreted directly during translation. Consider three possible benefits of the more roundabout method for protein secretion versus the simpler, more straightforward approach indicated.
The following results were obtained in early studies on the translation of secretory proteins. Based on what we now know of this process, explain the reason why each result was observed.a. An in vitro translation system consisting only of mRNA and ribosomes resulted in secretory proteins that were larger than the identical protein when translated in a cell.b. A similar system that also included microsomes produced secretory proteins that were identical in size to those found in a cell.c. When the microsomes were added after in vitro translation, the synthesized proteins were again larger than those made in a cell.
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