BIOL 1090 Lecture Notes - Lecture 17: Endomembrane System, Lipid Bilayer, Lysosome

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purplewombat479

16 Dec 2017

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Er function: protein translation: all protein translation begins on free ribosomes. Translation is completed in 1 of 2 ways: translation completed in free ribosomes, cytosolic proteins, peripheral membrane proteins, these proteins can be targeted to nucleus, mitochondria, peroxisomes, chloroplasts, translation completed by ribosomes attached to er membrane (rough er) Ribosomes are targeted to the er membrane by a signal sequence" in the protein being translated. Signal sequence" located at amino n-terminus contains 6-15 consecutive hydrophobic amino acids. Proteins moves through channel into er as it is being synthesized = co-translational import. Protein synthesis resumes: polypeptide enters the er (through the translocon) as it is translated. Initially, translation is the same as for secretory proteins. Protein being formed doesn"t pass completely through the translocon: nascent polypeptide contains stop-transfer sequences = hydrophobic transmembrane domain (tmd) Translocon opens laterally and inserts tmd of nascent polypeptide into lipid bilayer of.

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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

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

QUESTION 30

The function of centrosome is:

	1.	Microtubule initiation and organization in animal cells
	2.	Organization of thin filaments
	3.	Depolymerization of microtubules
	4.	Organization of intermediate filaments

2.5 points

QUESTION 31

The destinations of proteins synthesized on "free" ribomsomes include:

	1.	Endoplasmic reticulum
	2.	Nucleus
	3.	Mitochondria
	4.	Lysosomes

2.5 points

QUESTION 32

Microtubules can be assembled and disassembled quickly in response to the cellular changes is because:

	1.	Cells synthesize tubulin proteins very fast.
	2.	Cells can turn other cytoskeletal filaments into microtubules
	3.	Microtubules have an instable plus end and microtubules are probably organized by weak non-covalent interactions
	4.	The motor proteins of microtubules can organize the microtubules in response to the cellular changes

2.5 points

QUESTION 33

Both signal recognition particle and a translocon in rough endoplasmic reticulum membrane can recognize and bind to the signal sequence of a secretory protein, so they play the exact same role during protein co-translational translocation.

True

False

2.5 points

QUESTION 34

Rough endoplasmic reticulum is so named is because:

	1.	It has many proteins associated with its surface.
	2.	It has ribosomes associated with its cytosolic surface.
	3.	It is associated with nuclear membrane.
	4.	It has vesicles budding off its surface.

2.5 points

QUESTION 35

The membrane vesicles that transport materials between membrane compartments have a protein coat. The protein coat has similar functions in different vesicles. These functions include:

	1.	Help the enclosed material fold correctly.
	2.	Help degrade the protein in the vesicles
	3.	Maintain the internal pH of the vesicles
	4.	Function as mechanical device to form a vesicle and select the components to be carried by a vesicle.

2.5 points

QUESTION 36

Lysosomes are important for:

	1.	Receptor-mediated endocytosis.
	2.	Breaking down foreign particles brought into the cells by endosomes
	3.	Regulating the process of organelle turnover.
	4.	Protein trafficking between membrane compartments

2.5 points

QUESTION 37

Which of the following is correct about membrane biosynthesis?

	1.	Membranes are synthesized in Golgi Complex.
	2.	Membranes arise from preexisting endoplasmic reticulum membranes.
	3.	Membranes are synthesized on ribosomes.
	4.	Membranes of all organelles have the same composition of proteins and lipids, since they all originate from endoplasmic reticulum.

2.5 points

QUESTION 38

During skeletal muscle contractions, the shortening of the muscle fibers is because of:

		The shortening of the thin and thick myofilaments.
		The shortening of the cytoskeletal filaments.
		The kinesin proteins moving over microtubules.
		The actin and myosin filaments sliding over each other.

2.5 points

QUESTION 39

The assembly and disassembly of microtubules is regulated by rate of growth and shrinkage of the plus end.

True

False

2.5 points

QUESTION 40

The functions of Golgi complex include:

	1.	O-linked oligosaccharides and most of a cellâs complex polysaccharides are assembled in Golgi complex
	2.	Cis Golgi complex sorts proteins
	3.	Trans Golgi complex segregates proteins in different types of vesicles for dilevery.
	4.	N-linked oligosaccharides are further processed in Golgi complex

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BIOL 1090 Lecture Notes - Lecture 17: Endomembrane System, Lipid Bilayer, Lysosome

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