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ololo11 [35]
3 years ago
8

Myosin from a rabbit will bind to actin from an amoeba. What does this suggest about the evolution of the structures of actin an

d myosin?
Biology
1 answer:
Vikentia [17]3 years ago
4 0

Answer:

Actin accounts for the fact that in the protein content of a cell it always represents a high percentage and its sequence is very conserved, that is, it has changed very little throughout evolution.2 3 For both reasons it can be said That its structure has been optimized. Two peculiar characteristics can be highlighted on this: it is an enzyme that hydrolyzes ATP, the "universal currency of energy" of biological processes, doing so very slowly. But at the same time it needs that molecule to maintain its structural integrity. It acquires its effective form in an almost dedicated folding process. It is also the one that establishes more interactions with other proteins of how many are found, which allows it to perform the most varied functions that reach almost all aspects of cell life. Myosin is an example of a protein that binds actin. Another example is viline, which can interweave actin into bundles or cut actin filaments, affect the concentration of calcium cation in its environment.4

Forming microfilaments in a dynamic process provides a scaffolding that gives the cell a way to quickly remodel in response to its environment or body signals, for example, improves the cell surface for absorption or adhesion supports cells to form tissues. Other enzymes, organelles such as cilia, can be anchored on this scaffold, directing the deformation of the external cell membrane that allows cell ingestion or cytokinesis. It can also produce movement, either by itself or by molecular motors. Thus contributing to processes such as intracellular transport of vesicles and organelles and muscle contraction, or cell migration, important in embryonic development, wound repair or cancer invasiveness. The evolutionary origin of this protein can be traced in prokaryotic cells, where equivalents exist. Finally it is important in the control of gene expression.

A good number of diseases are based on genetic alterations in alleles of the genes that govern the production of actin or its associated proteins, being also essential in the process of infection of some pathogenic microorganisms. Mutations in the different actin genes present in humans cause myopathies, variations in cardiac size and function and deafness. The components of the cytoskeleton are also related to the pathogenicity of intracellular bacteria and viruses, especially in processes related to the evasion of the immune system response

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ryzh [129]
All the deserts are found at 30<span>°N because


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3 years ago
For both actin and microtubule polymerization, nucleotide hydrolysis is important for ______. Group of answer choices promoting
jarptica [38.1K]

Answer:

For both actin and microtubule polymerization, nucleotide hydrolysis is important for decreasing the binding strength between subunits on filaments.

Explanation:

Cytoskeletal filaments are common to eucaryotic cells and are impotartant to the spatial organization of cells. Intermediate filaments provide mechanical strength and resistance to shear stress. Microtubules determine the positions of membrane-enclosed organelles and direct intracellular transport. Actin filaments determine the shape of the cell's surface and are necessary for whole-cell locomotion. A large number of accessory proteins are present that link the filaments to other cell components, as well as to each other. Accessory proteins are essential for the assembly of the cytoskeletal filaments in particular locations, and it includes the motor proteins that either move organelles along the filaments or move the filaments themselves.

Actin filaments and microtubules are assembled with expenditure of energy i.e the ATP/GTP tightly bound to actin/tubulin is irreversibly hydrolyzed to ADP/GTP during the assembly process, and liberation of Pi in the medium occurs subsequent to the incorporation of subunits in the polymer. Pi release acts as a switch, causing the destabilization of protein-protein interactions in the polymer, therefore regulating the dynamics of these fibres. The progress is made in four areas: the chemistry of the NTPase reaction; the structure of the intermediates in nucleotide hydrolysis and the nature of the conformational switch; the regulation of parameters involved in dynamic instability of microtubules; and the possible involvement of nucleotide hydrolysis in the macroscopic organization of these polymers in highly concentrated solutions, compared with the simple case of a equilibrium polymers.  

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3 years ago
3.Why is the surface of the Earth in constant motion?
tekilochka [14]
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14. 
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Answer:

sorry don't know sorry

Explanation:

ok

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