Life: The Science of Biology
11th Edition
ISBN: 9781319010164
Author: David E. Sadava, David M. Hillis, H. Craig Heller, Sally D. Hacker
Publisher: W. H. Freeman
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Chapter 19.2, Problem 3R
Summary Introduction
To review:
The situation when MyoD (for myoblast-determining gene) in the undifferentiated myoblasts was inserted and over expressed.
Introduction:
MyoD or the myoblast determining gene has a role in the formation of muscles in the body. For the formation of the muscles, differentiation has to occur. The differentiation process can only occur after the cell cycle has terminated. With the ongoing cell cycle process, differentiation cannot take place.
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Explain the basis for coiling of alpha-helices in the tail of myosin and its relationship to the number of amino acids per turn of the alpha helix.
Briefly describe an in vitro experiment that differentiate between the Arp2/3 complex’ ability to associate with both the side of the ‘mother’ actin filament and with the barbed end of the ‘mother’ actin filament. Your experiment should take advantage of capping protein (binds and blocks barbed ends), and direct visualization of actin filaments.
Draw diagrams of actin filaments (simple lines are okay) that indicate the possible outcomes of your experiment.
describe your interpretation of the possible outcomes for the mechanism of Arp2/3 complex-mediated branch formation
1. Which myosin type II property is most different from kinesin-1?
A) myosin has two heads that can bind to cytoskeletal filamentsB) myosin is recruited into thick bipolar assembliesC) myosin hydrolyzes ATPD) myosin is an allosteric motor
2. If you were examining a newly available genome and your task was to identify the encoded family of kinesin motor proteins, what domain would be the most useful starting place for your analysis?
A) Light chain #1 binding sitesB) Neck regionC) Cargo domainD) Motor domainE) Light chain #2 binding sites
please explain
Chapter 19 Solutions
Life: The Science of Biology
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- Detailed measurements of sarcomere length andtension during isometric contraction in striated muscleprovided crucial early support for the sliding-filamentmodel of muscle contraction. Based on your understand-ing of the sliding-filament model and the structure of asarcomere, propose a molecular explanation for the rela-tionship of tension to sarcomere length in the portions ofFigure Q16–1 marked I, II, III, and IV. (In this muscle, thelength of the myosin filament is 1.6 μm, and the lengths ofthe actin thin filaments that project from the Z discs are 1.0μm.)arrow_forwardNeurofilament proteins assemble into long, intermediate filaments , found in abundance running along the length of nerve cell axons. The C-terminal region of these proteins is an unstructured polypeptide, hundreds of amino acids long and heavily modified by the addition of phosphate groups. The term “polymer brush” has been applied to this part of the neurofilament. can you suggest why?arrow_forwardThe diagram shown represents the coding strand of the myosin gene. Mutations in myosin can lead to muscle defects during development. Using what you know about how mutations can affect transcriptional and post-transcriptional regulation, match the results shown on the Northern (mature mRNA) to the mutations shown. The N lane shows the size and amount expected for non-mutated myosin mRNA. All samples were loaded at the top (-) side of the gel. Part 1. Which lane or lanes on the gel could be the result of mutation A? --4 ТАТАА AUG UAA Only known regulatory region TSS Mutation B: Mutation C. A: 5-base 20 nucleotides 3 nucleotides deletion deleted changed N 1 2 3 4 5arrow_forward
- The diagram shown represents the coding strand of the myosin gene. Mutations in myosin can lead to muscle defects during development. Using what you know about how mutations can affect transcriptional and post-transcriptional regulation, match the results shown on the Northern (mature mRNA) to the mutations shown. The N lane shows the size and amount expected for non-mutated myosin mRNA. All samples were loaded at the top (-) side of the gel. Part 1. Which lane or lanes on the gel could be the result of mutation A? 00000 I lane 1 lane 2 lane 3 lane 4 lane 5 TATAA Mutation A. Deletion of indicated 2 nucleotides AUG TSS Mutation B. Deletion of 150 nucleotides N 1 2 3 4 5 UAA Mutation C. 3 nucleotides changedarrow_forwardThe diagram shown represents the coding strand of the myosin gene. Mutations in myosin can lead to muscle defects during development. Using what you know about how mutations can affect transcriptional and post-transcriptional regulation, match the results shown on the Northern (mature mRNA) to the mutations shown. The N lane shows the size and amount expected for non-mutated myosin mRNA. All samples were loaded at the top (-) side of the gel. Part 1. Which lane or lanes on the gel could be the result of mutation A? ТАТА AUG UAA Only known regulatory region TSS Mutation B: Mutation C. 3 nucleotides 20 nucleotides deleted A: 5-base deletion changed 1 2 4 5 lane 1 lane 2 lane 3 lane 4 lane 5 OOO0Oarrow_forward2,3-Butanedione monoxime (BDM) inhibits the action of myosin. Plese list three processes in a plant cell that would be disrupted if myosin is inhibited. Explain why?arrow_forward
- The Arp2/3 complex makes branched actin filaments by associating with a ‘mother’ actin filament and initiating assembly of a ‘daughter’ actin filament. Although it has been thought that Arp2/3 complex associates with and makes branches from the side of the ‘mother’ actin filament, it is alternatively possible that Arp2/3 complex associates with and makes branches from the barbed end of the ‘mother’ actin filament. Design an in vitro experiment (with purified proteins, such as actin and Arp2/3 complex) to determine which of these possibilities is correct by taking advantage of capping protein (binds and blocks barbed ends), and direct visualization of actin filaments. (1) Briefly describe your experiment in no more than three sentences (2) Draw diagrams of what the arrangement of actin filaments (simple lines are okay) are expected to look like in your proposed experimental and control conditions that indicate the possible outcomes of your experiment (3) Briefly describe your…arrow_forwardWhy the process of DNA is transcribed into mRNA and then translated into protein is referred to as the “central dogma” of biology? Give one scenario that would explain how a mutation in the DNA of the Piedmontese bull could lead to muscle hypertrophy. If more cows had the same musculature as the Piedmontese bull, how would that affect meat production in countries that use cows as a primary meat source?arrow_forwardProtein-X has a calcium (Ca²+)-binding regulatory subunit. Upon calcium (Ca²+) binding the protein changes its own conformation resulting in the conformation change of protein-Y. As a result of this calcium (Ca²+)-dependent protein-X mediated conformational change protein-Y exposes the myosin II head binding sites on the skeletal muscle actin filaments. Identify the protein-X and protein-Y from the following choices. O Protein-X: Troponin; Protein-Y: Tropomysosin O Protein-X: Tropomodulin; CapZ O Protein-X: Nebulin; Protein-Y: Titin Protein-X: Tropomysosin; Protein-Y: Tropomodulinarrow_forward
- You are growing up myoblasts, C2C12 cells, to use in a myogenic study. You are using T-150 flasks with a culture area of 150 cm2 and when confluent contains 2 x 107 cells.You are growing up myoblasts ) If 20% of a culture of human cells have a DNA content somewhere between 1&2*s (S-phase=8 hours) and 1X amount of DNA in non-dividing cells. What is the generation time?arrow_forwardThe concentration of actin in cells is 50–100 timesgreater than the critical concentration observed for pureactin in a test tube. How is this possible? What prevents theactin subunits in cells from polymerizing into filaments?Why is it advantageous to the cell to maintain such a largepool of actin subunits?arrow_forwardExplain why there are no known motors that use intermediate filaments as tracks.arrow_forward
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