Imagine a protein that normally resides and functions in the ER lumen. What would be the fate of this protein in a biological cell which has its SRP gene mutated such that it does not recognize the ER signal sequence? The protein would reside in the nucleus. O The protein would reside in the ER. O The protein would reside in the cytoplasm. The protein would reside in the nucleus.

Imagine a protein that normally resides and functions in the ER lumen. What would be the fate of this protein in a biological cell which has its SRP gene mutated such that it does not recognize the ER signal sequence? The protein would reside in the nucleus. O The protein would reside in the ER. O The protein would reside in the cytoplasm. The protein would reside in the nucleus.

Concepts of Biology

1st Edition

ISBN:9781938168116

Author:Samantha Fowler, Rebecca Roush, James Wise

Publisher:Samantha Fowler, Rebecca Roush, James Wise

Chapter9: Molecular Biology

Section: Chapter Questions

Problem 10RQ: Control of gene expression in eukaryotic cells occurs at which level(s)? a. only the transcriptional...

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Imagine a protein that normally functions in the nucleus. If you added an ER signal sequence to the N-terminal end of the gene that expresses this nuclear protein (through genetic manipulation), what would be the fate of the expressed protein? The protein would reside in the cytoplasm. The protein would reside in the cell membrane. The protein would reside in the ER. The protein would reside in the nucleus.
A KDEL sequence is necessary for ... Select an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer. a lysosomal enzymes to reach the lysosome. b transmembrane proteins to be targeted to the plasma membrane. с binding to KDEL receptors and transport through the trans-Golgi network. the transport of resident ER proteins from the Golgi to the ER.
Hac1 is another chaperone protein that is up-regulated in response to unfolded proteins in the ER. You detect amounts of Hac1 mRNA and protein in the absence and presence of unfolded protein in the ER of a eukaryotic cell as shown in the figure below. b. Describe two specific biological processes that the cell could regulate in order to increase the amount of Hac1 protein. Briefly explain your answer using the information from figure C & D. Hac1 MRNA expression Hac1 protein expression Unfolded proteins in ER No unfolded No unfolded proteins In ER Unfolded protelns in ER proteins in ER
Given the following schematic for a gene and its associated regulatory regions, answer the following questions by placing the correct letter in the provided blanks please put in the correct letter for the questions What region would provide cell type-specific expression of genes? region What site would significantly increase gene expression rates? = region What region or regions of this gene’s coding sequence are expressed as amino acids = region
When high levels of unfolded proteins are detected in the endoplasmic reticulum (ER), a eukaryotic cell responds by increasing the gene expression of chaperone proteins, which help proteins to fold correctly. BiP is a chaperone protein. You detect amounts of BiP mRNA and protein in the absence and presence of unfolded protein in the ER of a eukaryotic cell as shown in the figure below. a. Describe two specific biological processes that the cell could regulate in order to increase the amount of BiP protein. Briefly explain your answer using the information from figures A & B. A BİP MRNA expression В BiP protein expression No unfolded Unfolded No unfolded Unfolded proteins in ER proteins in ER proteins in ER proteins in ER
When high levels of unfolded proteins are detected in the endoplasmic reticulum (ER), a eukaryotic cell responds by increasing the gene expression of chaperone proteins, which help proteins to fold correctly. BiP is a chaperone protein. You detect amounts of BiP mRNA and protein in the absence and presence of unfolded protein in the ER of a eukaryotic cell as shown in the figure below. a. Describe two specific biological processes that the cell could regulate in order to increase the amount of BiP protein. Briefly explain your answer using the information from figures A & B. A BİP MRNA expression BiP protein expression No unfolded Unfolded No unfolded Unfolded proteins in ER proteins in ER proteins in ER proteins in ER
Control of gene expression in eukaryotic cells occurs at which level(s)? a. only the transcriptional level b. epigenetic and transcriptional levels c. epigenetic, transcriptional, and translational levels d. epigenetic, transcriptional, post-transcriptional, translational, and post-translational levels
This figure below shows the organization of a protein that will end up in the ER membrane . The N-term and C-termini of the protein are labeled. Boxes 1,2, and 3 represent membrane spanning sequences. Non-membrane-spanning regions are labeled X, Y and Z. Once this protein is fully translocated , where will region Z end up? signal peptidase cleavage site NE O inserted in the ER membrane in the ER lumen O in the cytoplasm degraded by a signal peptidase
please help
Below is a model of a signal transduction pathway that results in the transcribing of mRNA: Receptor protein Transcription factor Phosphorylation cascade DNA mRNA What is the best description of what would happen if the phosphorylation cascade resulted in a phosphate being attached to the transcription factor? O mRN would not stop being transcribed from the DNA. O The phosphorylation cascade would continue to release excess phosphates. O mRNA would stop being translated from the DNA. O Receptor proteins would not bind to the signaling hormone.
What will happen if both SRP54 and SRalpha are bound to GTPgammaS instead of GTP? SRP54 and SRalpha will always bind to the sec61 translocon, and ribosome will fail to translate proteins into the ER lumen SRP54 will never bind to SRP receptor, and ribosome will always translate proteins into the ER lumen SRP54 and SRalpha will always bind to the sec61 translocon, and ribosome will always translate proteins into the ER lumen SRP54 will never bind to SRP receptor, and ribosome will fail to translate proteins into the ER lumen
Imagine that you are working with DNA sequences of soluble proteins (not membrane proteins) and have the technology to genetically engineer/alter the existing sequence and you can express this particular protein in a yeast cell model. You also have the power to track and visualize where the genetically engineered proteins traffic in your model system. You engineer an ER signal sequence to the carboxyl-terminal end of a normally cytosolic protein. Which best describes the fate of this protein? O The protein is translocated through the ER membrane translocon channel, N' end first O The protein is translocated through the ER membrane translocon channel, C' end first The protein is degraded The protein remains in the cytosol