BIO 1140 Lecture Notes - Lecture 65: Hayflick Limit, Telomere, Phospholipase A2

16 views2 pages

olivefox459

24 Aug 2016

School

University of Ottawa

Department

Biology

Course

BIO 1140

Professor

Caroline Petit- Turcotte

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

Document Summary

A mutation in the gene for the signal peptidase prevents the protein from being able to cleave signal sequence peptides. Co-translation to make transmembrane proteins and soluble proteins to be placed in the er to the golgi secreted in a vesicle. Missense: change in a base pair that would lead to a change in the amino acid sequence that will change it. Not nonsense because it would not get to the er membrane. Peptidase is what the ribosome binds to on the membrane on the rough endoplasmic reticulum during co translation. Translation will still occur, but the polypeptide will remain attached and will not make it to the lumen and posttranslational things will not occur. Signal peptidase cleaves the signal peptide but if this does not occur it will remain attached to the signal peptidase. As microtubules slide past each other, motor proteins push on the chromatids as if it were cargo.

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

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

goldmanatee250

1/What is the fate of a protein with no N-terminus Signal Sequence?

(a)Transport through the constitutive secretory pathway

(b)Dispersal throughout the cytoplasm

(c)Transport into the nucleus

(d)Transport to the rough endoplasmic reticulum (RER)

2/ In nerve cells, Botulinum toxin-A degrades a subunit of a T-snare localized on the plasma membrane, how would this affect vesicular trafficking?

(a) It blocks the co-translational import of neurotransmitter proteins into the Endoplasmic reticulum via the translocon.

(b) It prevents the addition of carbohydrates to translated proteins

(c)It blocks the fusion of neurotransmitter-containing vesicles with the plasma membrane because theT-snare would not be able tophysically interact with the V-snare.

(d) None of the above

What is the correct order of events of Clathrin-mediated endocytosis?

1. Uncoating of Clathrin- coated vesicle

2. Recruitment of Clathrin and selection of cargo

3. Fusion of vesicle with early endosome

(a) 1, 2, 3

(b) 2, 1, 3

(d) 3, 1, 2

4/ Vesicles traveling anterogradely will eventually fuse with the cell membrane.

Which of the following elements does NOT participate in the fusion event?

(a) v-snare

(b) t-snare

(d) clathrin coat protein

When a cell releases a hormone into the bloodstream and a number of cells in a

distal location respond, this type of signaling is...

(a) Autocrine signaling

(b) Endocrine signaling

(d) Juxtacrine signaling

taupereindeer397

BIO 1140 Lecture Notes - Lecture 65: Hayflick Limit, Telomere, Phospholipase A2

Document Summary

Get access

Related textbook solutions

Molecular Cell Biology

Biology: Science for Life with Physiology

Concepts of Biology

Biology

Essentials of Biology

Related Documents

BIO 1140 Lecture Notes - Lecture 16: Signal Peptidase, Translocator Protein, Transmembrane Protein

BIO 1140 Lecture Notes - Lecture 24: Phospholipase C, Signal Transduction, Insulin

BIO 1140 Lecture Notes - Lecture 17: Stop Codon, Reading Frame, Signal Transduction

Related Questions