BIO 1140 Lecture Notes - Lecture 17: Signal Recognition Particle, Signal Peptidase, Cytosol

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magentawolf8

8 Nov 2016

School

University of Ottawa

Department

Biology

Course

BIO 1140

Professor

Caroline Petit- Turcotte

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Document Summary

Bio - lec 17 - translation and protein sorting. Soluble protein (that will remain in the cytosol) will be translated using free cytosolic ribosomes. Temporarily blocks translation before it docks the ribosome to the er membrane co translation (secreted) : Import protein across the membrane as its being translated. Ribosomes are in cytosol, get them to the rough er. Beginning sequence of peptide (signal seqeuncing), used to recognize that these proteins are part of the membrane. Signal recognition particle (in cytosol), looks for beacon (signal sequences as they"re extending from the ribosome), and they bind to them. So that once translation resumes, it grows through the pore into the er. Signal peptidase : signal peptidase cleaves the signal sequence peptide from the growing polypeptide and will be available to co-translate another protein, leaving you with the actual protein. Translation of the mrna complete; ribosomal subunits are recycled. Result : polypeptide free inside the er lumen.

Related Questions

1. Which cytosolic factor is most likely to associate with the signal sequence of a protein that is targeted co-translationally to the ER?

A chaperone of the Hsp70 family

The translocation channel

The ribosome

Signal recognition particle (SRP)

Signal peptidase

2. What is the most likely fate of a protein with an N-terminal hydrophobic sorting signal and an additional internal hydrophobic domain of 22 amino acids?

The protein stays in the cytosol

The protein is transported to mitochondria

Because the protein has an N-terminal sorting signal, the protein is translocated all the way into the ER lumen

The hydrophobic domain is recognized as a transmembrane domain once it is in the translocation channel and released sideways into the membrane

The hydrophobic domain is cleaved off by signal peptidase

3. Which of the following statements best describes N-glycosylation? N-glycosylation refers to........

the addition of a pre-formed sugar tree to a serine or threonine present in the cytosolic domain of a protein

the addition of a pre-formed sugar tree to a phospholipid to make a glycolipid

the addition of individual sugars to selected amino acids on a protein

the addition of a pre-formed sugar tree to an asparagine residue found within the consensus sequence Asn-X-Ser/Thr in an ER lumenal domain of a protein

the addition of a pre-formed sugar tree to an asparagine residue found within the consensus sequence Asn-X-Ser/Thr in a cytosolic domain of a protein

4. What is the most likely fate of a protein in which a mutation has led to misfolding in the ER?

It is sequestered by the proteasome in the cytosol

It is first tagged with ubiquitin in the ER and then degraded by the proteasome in the cytosol

It is first moved out of the ER, tagged with ubiquitin in the cytosol and then degraded by the proteasome in the cytosol

It associates with many chaperones in the ER, which guarantee its correct folding

Its misfolded state is recognized by chaperones in the ER, which will induce the protein's degradation by the proteasome in the ER.

raspberrybeaver682

29 Most proteins destined to enter the endoplasmic reticulum _________.

(a) are transported across the membrane after their synthesis is complete.

(b) are synthesized on free ribosomes in the cytosol.

(d) are keep binding to Signal recognition particle (SRP) while they are translated.

30 Which of the following choices reflects the appropriate order of locations through which a protein destined for the plasma membrane travels?

(a) lysosome â endosome â plasma membrane

(b) ER â lysosome â plasma membrane

(d) ER â Golgi â plasma membrane

31 Which of the following statements about vesicle budding from the Golgi is false?

(a) COPII can initiate vesicle budding on Golgi membrane.

(b) Some vesicles budded from Golgi membranes move towards ER.

(d) Clathrin molecules act at the cytosolic surface of the Golgi membrane.

32 Which of the following statements is false?

(a) The signal sequences on mitochondrial proteins are first bound to translocator on outer membrane after translation.

(b) Most mitochondrial proteins are not imported from the cytosol but are synthesized inside the mitochondria.

(c) Chaperone proteins in the mitochondria facilitate the movement of proteins across the outer and inner mitochondrial membranes.

(d) Mitochondrial proteins cross the membrane in their unfolded state.

orangeplatypus673

6. True or false

a_______ Nuclear pore complexes are specialized so that some mediate import and others mediate export

b_______ Membrane-bound and free ribosomes, which are structurally and functionally identical, differ only in the proteins they happen to be making at a particular time.

c_______ Some proteins can be made as either free or membrane-bound proteins. They have the same mRNA but different splicing and poly-adenylation patterns

d_______ a protein that does not have a sorting signal will be tagged for destruction by ubiquitin

e_______ when the hydrophobic signal peptide emerges from the ribosome, it is bound by SRP, which causes a pause in protein synthesis. Synthesis resumes when the ribosome with a bound SRP then binds to the SRP receptor on the cytosolic surface of the rough ER.

f________ A protein cannot leave the ER unless it is correctly folded

g________ All of the glycoproteins and glycolipids in intracellular membranes have their oligosaccharide chains facing the cytosolic side, and all those in the plasma membrane have their oligosaccharide chains facing the outside of the cell.

BIO 1140 Lecture Notes - Lecture 17: Signal Recognition Particle, Signal Peptidase, Cytosol

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