Log in
HomeClass Notes1,200,000CA670,000

Biology 1002B Lecture Notes - Lecture 7: Signal Recognition Particle, Signal Peptide, Secretion

24 views6 pages
School
Western University
Department
Biology
Course
Biology 1002B
Professor
Haffie

For unlimited access to Class Notes, a Class+ subscription is required.

Document Summary

Any protein that interacts with the plasma membrane goes through the secretory pathway. That means they are all synthesized on ribosomes that attach to the er. They are transiently attached to the er, this means. If the protein is going to the plasma membrane, it has to be targeted to the er. The signal peptide tells the cell what it is destined for, tells the cell that this is going to the er. The signal recognition particle pulls the ribosome and the partially translated protein to the er. The signal peptide is part of the protein. When the mrna gets translated, it has info that makes this signal peptide (which is in the mrna), so this info is too in the gene. The gene that encodes this protein has sequences for the sp (not added on, part of it) The two join, and then translation continues.

Get access

Grade+
$40 USD/m
Billed monthly
Grade+
Homework Help
Study Guides
Textbook Solutions
Class Notes
Textbook Notes
Booster Class
10 Verified Answers
Class+
$30 USD/m
Billed monthly
Class+
Homework Help
Study Guides
Textbook Solutions
Class Notes
Textbook Notes
Booster Class
7 Verified Answers

Related Documents

Biology 1002B Lecture Notes - Fall 2018 Lecture 7 - Chlamydomonas, Membrane structure, ATP-binding cassette transporter
greyyak215
Biology 1002B Lecture Notes - Lecture 7: Osmosis, Membrane Transport, Peptide
beigecrab253
Biology 1002B Lecture 5: Lec 5 - Membrane Biology
sapphirebear815

Related Questions

1. The histones that form the core of the nucleosome get into the nucleus by which of the following?

a) Passive diffusion through nuclear pores

b) Selective and facilitated active transport through nuclear pores

c) Ribosomes located in the nucleus synthetize histones in the nucleus

d) Histones are made at the ER membrane and then diffuse to the nucleus

2. Membrane proteins that belong to the golgi, lysosome, or plasma membrane first pass through which organelle before reaching their final subcellular destination?

a) The golgi apparatus

b) The smooth ER

c) The nucleus

d) The ER membrane

e) The ER lumen

3. Where in the cell would a ribosomal protein be located if it has had its nuclear export signal inactivated (non-functional or non-existent).

a) The protein would be found in the ER lumen

b) The protein would remain in the nucleus

c) The protein would be secreted

d) The protein would remain in the cytoplasm

e) The protein would be in the ER membrane

4. Where would be the final destination of a protein if it contained a NLS anywhere in the protein sequence (and which is exposed to the cytoplasm after protein folding) but also contained an ER signal sequence at the carboxy terminus?

a) The ER lumen

b) The nucleus

c) The cytoplasm

d) The inner nuclear membrane

e) The ER membrane

5. The sequence K-D-E-L serves as a retention/retrieval signal for ER proteins.

a) True

b) False

6. The following are true for both cell membrane proteins and secretory proteins EXCEPT?

a) Precursors of the mature proteins contain signal sequence.

b) Both types of proteins contain stop-transfer sequences

c) Both types of proteins enter the ER while being synthetized

d) Both types of proteins pas through the golgi apparatus

e) Both are carried by clatherin-coated vesicles

7. If you isolate a regulated secreted protein from a secretory/storage vesicle and inject it into the cytosol, is will?

a) Be secreted through channels in the plasma membrane

b) Be taken up into secretory vesicle and secreted

c) Remain in the cytosol until it is degraded

d) Be taken up into the rough ER and follow the secretory pathway

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.

Some cells in plant and animals are specialized for the production and release of a particular chemical, often a protein or some other regulatory molecule. These cells generally produce and release their product only when the proper signal is present. Describe the series of events in this cell that would lead from the perception of this signal to the release of the desired product. Begin by providing specific information on: 1) the transduction of the signal across the membrane by the G protein system with subsequent release of the appropriate second messenger(s); 2) the process by which the signal is amplified by the MAP kinase pathway; 3) how the product(s) produced by the MAP kinase cascade reach the nucleus to initiate the transcription of the relevant gene(s).

Assume now that transcription has already occurred, that a mature mRNA has been produced in the nucleus and has migrated to the cytosol, and that this mRNA has been recruited by a ribosome to initiate translation. Since the protein product is secretory, synthesis of the protein will be associated with the rough endoplasmic reticulum. Continue by providing information on 4) how the free ribosome becomes associated with the endoplasmic reticulum to allow for the release of the synthesized protein into the rough ER; 5) the modification or processing of the protein that occurs in the endoplasmic reticulum; 6) the packaging and/or modification of the protein for transport from the ER to the Golgi apparatus; 7) the modification, processing, and packaging of the protein in the Golgi apparatus; and 8) the steps leading to the eventual release of the target protein from the cell via exocytosis.