You are studying a eukaryotic protein PKK in the lab.You fuse the DNA encoding GFP (green fluorescent protein) to the C terminus of thePKK gene.You also create the following GFP-PKK variantsWild- type: N--GFPSignal sequence Transmembrane domainKinase domainVariant 1: N--GFPTransmembrane domainKinase domainVariant 2: N-GFPSignal sequence Transmembrane domainVariant 3:N-GFPSignal sequence Kinase domainVariant 4:-GFPKinase domainIf you examine PKK variant 4 trafficking in a eukaryotic cell, which of the followingare true?Select all that applyThis fusion protein will be made as a cytosolic proteinThis fusion protein will not function like the wild-type proteinThis fusion protein will traffic to the cell membraneThis fusion protein will not traffic to the cell membrane

Proteins synthesized through translation process is directed to specific locations in the cells.…

Answered: You are studying a eukaryotic protein…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Explain how plasma membrane proteins that start to be translated in the cytosol are then targeted to the ER during translation. I am looking for two things that are required here.
The figure from Moore (2020) shows a G protein-coupled receptor in a membrane. Note that "out" means outside the cell and "in" means facing the cytoplasm. The three amino acids "DRY" in loop I2 are required for protein targeting. What is the name of this kind of sequence, and what is its function? What protein targeting sequence is no longer included in this diagram? Why? The sequence "QXXNK" (where X is any amino acid) found in loop I3 has been identified based on its enzymatic activity. What is this activity? What particular domain would you expect to find in either Loop E1, E2, or E3? The gene that codes for this protein is a member of a family of genes that has arisen over evolutionary time. If you compared several of the genes in this family, would you expect their sequences to be most homologous (similar) in the region you describe in #3 above or #4 above? Why?
please help me with this quickly
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Using a computer algorithm that searches for sequence similarities in other organisms, you discover that hexose kinase is a highly conserved gene that is expressed by many species, both prokaryotic and eukaryotic. The most closely related prokaryotic homolog of hexose kinase has a protein sequence in which 90% of the amino acids are identical to those of the human version of the gene. To learn more about their similarity at the DNA level, you obtain segments of the genomic DNA coding for the hexose kinase gene in both humans and this prokaryotic species. After combining both DNA samples, you heat them to denature the DNA strands and then allow them to cool and reanneal. Finally, you examine the DNA hybrids you obtain under the electron microscope. Practice Question 3 A) Your analysis reveals that there are three different DNA hybrids in this sample, these can be seen below. You reason that one must belong to the prokaryotic species, one to the humans and the third arose when one strand…
You just isolated a mutant in the eukaryotic organism C. elegans (aka the world's coolest model organism) that fails to transcribe your favorite gene. Which of the following region(s) are likely to contain your mutation? (You may choose more than one.) Group of answer choices Rut site -10 consensus sequence Rho protein TATA box Sigma subunit binding site Transcription start site
You plan to synthesize a peptide to be used as a vaccine to treat melanoma, a particularly aggressive form of skin cancer. Normally, gp100, a protein on the surface of melanocytes, activates cell growth when it is bound by its ligand. Activation of the growth pathway depends on the presence of threonine in the ligand. The effective peptide vaccine will mimic the natural ligand, but won’t cause cell growth and division. Below is the sequence of the natural ligand: LDMKTAG In order to ensure your newly designed peptide vaccine does not cause cell growth upon binding, you must substitute the Threonine residue at position 5. What amino acid would you replace it with, bearing in mind that the peptide should still be similar enough to bind to the gp100 protein in the surface of melanocytes. Explain your choice. Your vaccine will be administered as a topical cream, and you require your peptide to have an overall neutral charge in order to be functional. At what pH should you formulate…
ERAD, or ER associated degradation, is a quality control measure with the following function: A. misfolded proteins activate the expression of genes such as chaperones that will help to refold and stabilize misfolded proteins until the fold correctly B. proteins that cannot fold correctly are ejected from the ER through the translocon and degraded by the ubiquitin-proteasome system in the cytosol C. misfolded proteins are ubiquitinated and degraded by proteasomes inside the ER D. Unfolded proteins in the ER activate a transmembrane kinase in the ER that phosphorylates misfolded proteins that are sent to the lysosome in vesicles for degradation
You are studying a eukaryotic protein PKK in the lab. You fuse the DNA encoding GFP (green fluorescent protein) to the C terminus of the PKK gene. You also create the following GFP-PKK variants -GFP Wild- type: N- Signal sequence Transmembrane domain Kinase domain Variant 1: N- GFP Transmembrane domain Kinase domain Variant 2: N- -GFP Signal sequence Transmembrane domain Variant 3: N- -GFP Signal sequence Kinase domain Variant 4: N- -GFP Kinase domain If you examine wild-type PKK trafficking in a eukaryotic cell, which of the following are true? Select all that apply This fusion protein will be trafficked to the nucleus This fusion protein is a cell membrane protein This fusion protein will be trafficked to the Endoplasmic Reticulum This fusion protein is a nuclear protein
A KDEL sequence is a sequence of amino acids in a protein that binds a KDEL receptor, which helps recycle it back to the ER. Name two techniques a scientist could use in combination to experimentally demonstrate the function of a KDEL sequence. (To help you think about how to answer this: What would happen if the KDEL sequence were nonfunctional? How could you observe the result?) Please answer this and thank you!

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