gene for a eukaryotic polypeptide 300 amino acid residues Iong is altered so that a signal sequence recognized by SRP occurs at the polypeptide's amino terminus and a nuclear localization signal (NLS) occurs internally, beginning

gene for a eukaryotic polypeptide 300 amino acid residues Iong is altered so that a signal sequence recognized by SRP occurs at the polypeptide's amino terminus and a nuclear localization signal (NLS) occurs internally, beginning

Name: The gene for a eukaryotic polypeptide 300 amino acid residues Iong is
Uploaded: 2024-03-20T06:42:41.000Z
Channel: Bartleby
Description: The gene for a eukaryotic polypeptide 300 amino acid residues Iong is altered so that a signal sequence recognized by SRP occurs at the polypeptide's amino terminus and a nuclear localization signal (NLS) occurs internally, beginning at residue 150.

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter9: Gene Expression And Gene Regulation

Section: Chapter Questions

Problem 18QP: The following is a portion of a protein: met-trp-tyr-arg-gly-pro-thr-Various mutant forms of this...

See similar textbooks

Similar questions

The following is the only intron sequence of a gene that will be excised during the maturation of the mRNA. But it is not spliced in some tissues, where alternative splicing pattern is seen. Will the amino acid of its protein product following this sequence change? Explain with an example. ATGATAGCCAGACTCGCA
A synthetic mRNA added to a cell-free protein-synthesizing system produces a peptide with the following amino acid sequence: Met-ProIle-Ser-Ala. What would be the effect on translation if the following component were omitted from the cell-free protein-synthesizing system? What, if any, type of protein would be produced? Explain your reasoning. Q. GTP
Consider a transmembrane protein that forms a hydrophilic pore across the plasma membrane of a eukaryotic cell, allowing Na+ to enter the cell when it is activated upon binding a specific ligand on its extracellular side. It is made of five similar transmembrane subunits, each containing a membrane-spanning α helix with hydrophilic amino acid side chains on one surface of the helix and hydrophobic amino acid side chains on the opposite surface. Considering the function of the protein as a channel for Na+ ions to enter the cell, propose a possible arrangement of the five membrane-spanning α helices in the membrane.
ATM is a kinase that phosphorylates histone H2AX in response to double-stranded DNA breaks. Which of the following scenarios would most quickly regulate ATM activity in the cell? a) Adding silencing methyl groups to cytosines in the Atm gene b) Modifying the histone code for the Atm gene c) Increasing expression of a miRNA specific for the Atm mRNA d) Activating an E3 ubiquitin ligase specific for the ATM protein
Name two similarities and two differences between the cellular processes of importing protien into the ER and importing protein to the nucleus.
An integral membrane protein has an ER signal sequence near its N terminus and a stop transfer sequence in the middle. If a mutation removed the stop-transfer sequence, where would you expect to find the protein? Why?
The primary protein structure is shown in Figure 9-3(a).Where in the mRNA (near the 5′or 3′end) would a mutation in R2 be encoded?
A synthetic mRNA added to a cell-free protein-synthesizing system produces a peptide with the following amino acid sequence: Met-Pro- Ile-Ser-Ala. What would be the effect on translation if the following components were omitted from the cell-free protein-synthesizing system? What, if any, type of protein would be produced? Explain your reasoning. a. Initiation factor 3 b. Initiation factor 2 c. Elongation factor Tu d. Elongation factor G e. Release factors RF-1, RF-2, and RF-3 f. ATP g. GTP
The following is a portion of a protein: met-trp-tyr-arg-gly-pro-thr-Various mutant forms of this protein have been recovered. Using the normal and mutant sequences, determine the DNA and mRNA sequences that code for this portion of the protein, and explain each of the mutations. a. met-trp- b. met-cys-ile-val-val-leu-gln- c. met-trp-tyr-arg-ser-pro-thr- d. met-trp-tyr-arg-gly-ala-val-ile-ser-pro-thr-
If the coding region of a gene (the exons) contains 2,100 base pairs of DNA, would a missense mutation cause a protein to be shorter, longer, or the same length as the normal 700 amino acid proteins? What would be the effect of a nonsense mutation? A sense mutation?
EF-Tu, a member of the G-protein family, plays a crucial role in the elongation process of translation. Suppose that a slowly hydrolyzable analog of GTP were added to an elongating system. What would be the effect on the rate of protein synthesis?
Protein X is a soluble, secreted protein. It has an N-terminal ER import sequence that allows it to be translocated into the ER during translation. If you altered the sequence of this protein in the following ways, would it affect its final destination? If yes, explain why and what the new destination would be. If not, explain why. 1) You add an ER retention signal to the protein. 2) You add a nuclear localization signal to the end of the protein sequence.