MCB 2210 Lecture 10: Actin structure and introduction

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sapphiredog102

24 Oct 2016

School

UConn

Department

Molecular and Cell Biology

Course

MCB 2210

Professor

Daggett

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Document Summary

Beta and gamma actin in non-muscle cells. Structural features of actin: helical polymers composed of globular actin monomers that bind. Atp: actin monomer molecule is separates into two lobes by a deep cleft that binds atp or adp complexed with mg+2, actin exists in two forms in the cell: As a monomer called g- actin (globular actin) And as a filamentous polymer called f-actin (filamentous actin) F-actin is a helical polymer of g-actin subunits held together by non-covalent interactions. Polar polymer: the polarity of actin filaments can be determined by decorating the filaments with the actin-binding head domain of the myosin ii molecule (called sub fragment 1 or s1) When s1 is mixed with actin filaments, it attached to the sides at an angle, creating an arrow-head like pattern. One end is called the pointed end (minus - end) and the other is called the barbed end (plus + end)

Related Questions

1)Describe the directions in which the two motor proteins, kinesin and dynein, travel along a microtubule. Which of the two proteins moves materials towards the Golgi and which moves materials away from the Golgi? Lastly, what is the speed of kinesin dependent on?

2)What are microfilaments crucial for? How do they self-assemble? Which end do they prefer to elongate from?

3)Describe what types of filaments are in each of the bands of the sarcomere. As a muscle fiber is shortened, describe what happens to each of the bands in the sarcomere as the Z lines move inwards.

4)Describe the role of calcium ions in muscle contraction.

5)List the various types of actin-binding proteins

6) A. What are 3 functions of the cytoskeleton?

B.What are the three filaments that compose the cytoskeleton, and what are they composed?

7)How do they see the internal structures of cells in the microscope? What do proteins get labeled with?

8)Myosin II action (Figure 9.61) differs from that of kinesin (Figure 9.15) in that one of the kinesin heads is always in contact with a microtubule, whereas both myosin heads become completely detached from the actin filament. How are these differences correlated with the two types of motor activities in which these proteins engage?

9)If a myofibril were pulled so that the sarcomeres increased in length by approximately 50 percent, what effect would you expect this to have on the contractile ability of the myofibril? Why? What effects would this have on the H, A, and I bands?

10)Because cytoplasmic vesicles are seen to move in both directions within an axon, can you conclude that some microtubules are oriented with their plus end facing the axon terminus and others oriented with the opposite polarity? Why or why not?

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

ochrecoyote721

1. Kinesin-1 motors can move long distances on microtubule tracks without dissociating. By contrast, myosin II motors in skeletal muscle take only one or a few steps before letting go. What is most likely the difference between these two motors that allow two different types of movement?

A. Differences in length of the stalk of each respective motor allow for differences in step size

B. Differences in ATP versus GTP hydrolysis alter the motor head movement along filaments

C. Actin filaments are smaller in diameter and have less space for movement

D. Binding affinity of the Kinesin-1 motor head to microtubules is high, whereas binding affinity of the myosin II motor head to actin filaments is low

E. Microtubules are larger in diameter and have more space for movement

2. Dynamic instability causes microtubules either to grow or to shrink rapidly. What is the most likely reason for a microtubule to undergo rapid growth?

A. GTP hydrolysis exceeds the rate of heterodimer addition

B. GTP hydrolysis of alpha tubulin causes an outward bend in the heterodimer conformation

C. A low concentration of tubulin heterodimers are in solution

D. Heterodimer addition exceeds the rate of GTP hydrolysis

E. Increased trafficking of microtubule motor proteins favors stability

3. There are no known motor proteins that move on intermediate filaments (IFs). What property of intermediate filaments would most likely explain the lack of motor proteins?

A. Tissue specific expression of IFs prevent a single type of motor protein to evolve over time

B. Lateral bundling of IFs prevent motor movement

C. IFs are less dynamic than microtubules and actin filaments

D. IFs are unpolarized

E. IFs do not bind a nucleotide

4. You discover a mutation that results in less rapid hydrolysis of GTP by the beta-tubulin subunit. What would most likely occur?

A. There would be no change in filament assembly

B. There would be enhanced instability of the microtubule

C. There would be enhanced stability of the microtubule

D. Microtubules would not form

E. There would be enhanced treadmilling

5. Which of the following statements describes common features of cadherins and integrins?

A. They can link to microtubules using specific adapter proteins

B. They mediate heterophillic interactions

C. They achieve high binding affinity through clustering

D. They are responsible for interactions of a cell with the extracellular matrix

E. They are found in the apical plasma membrane of an epithelial cell

6. Intermediate filaments are uniquely non-polar and built by lateral bundling in five steps: 1) synthesis of an alpha-helical monomer, 2) formation of a coiled-coil dimer, 3) formation of a staggered tetramer of two coiled-coil dimers, 4) lateral association of 8 tetramers, and 5) addition of 8 tetramers to a growing filament. At what step is polarity lost?

A. Step 1

B. Step 2

C. Step 3

D. Step 4

E. Step 5

7. Collagenase is an enzyme that breaks peptide bonds in collagen to help destroy extracellular structures. What would be the most likely reason to use collagenase in a cell biology laboratory?

A. Disrupt cadherin interaction with the extracellular matrix

B. Disrupt cell-cell contacts to passage cells in cell culture

C. Dissociate epithelial cells from the underlying basement membrane to separate tissues

D. All of the answers are likely uses for collagenase

E. Lyse cells to expose intracellular proteins and organelles

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MCB 2210 Lecture 10: Actin structure and introduction

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