What will happen if both SRP54 and SRalpha are bound toGTPgammaS instead of GTP?SRP54 and SRalpha will always bind to the sec61 translocon, andribosome will fail to translate proteins into the ER lumenSRP54 will never bind to SRP receptor, and ribosome will alwaystranslate proteins into the ER lumenSRP54 and SRalpha will always bind to the sec61 translocon, andribosome will always translate proteins into the ER lumenSRP54 will never bind to SRP receptor, and ribosome will fail to translateproteins into the ER lumen

SRP54 and SRalpha are proteins involved in the process of protein synthesis and folding in the…

Answered: What will happen if both SRP54 and…

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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What does it usually mean when a microtubule has a GTP cap? O The microtubule has a ring of GTP added onto its plus end that acts to stabilize this end and prevent dynamic instability. O The microtubule has alpha and beta tubulin, both bound to GTP, at the plus end. The microtubule has alpha tubulin bound to GDP and beta tubulin bound to GTP at the plus end. O The microtubule is radiating from the MTOC where the minus ends are stabilized.
Which of the following small GTP-binding proteins does NOT play a role in cell migration during chemotaxis? O Cap Z Rho Cdc42 O All of the listed GTPases play a role in cell migration O Rac ◆ Previous
What would most likely occur to nuclear-cytoplasmic shuttling if the intrinsic GTPase activity of RAN was slowed down by 50%? Group of answer choices RAN would not bind exportin and proteins would accumulate in the nucleus All of the answers are likely None of the answers are likely Importin beta would not release from RAN in the cytoplasm and nuclear import would slow down RAN would not bind to importin beta and protein cargo in the nucleus would not release
Match the protein on the left with the mechanism of how the protein is activated on the right. Beclin-1 XBP-1s Rheb LC3 IRE-1 [Choose] [Choose] Phosphorylation Binding another protein to form a complex Dephosphorylation Cleavage Binding of GTP Dimerization Splicing in cytoplasm [Choose] [Choose]
TGF-B Receptor I (RI) phosphorylation of Smad2/3 does all of the following EXCEPT: activate Smad2/3 binding to the Co-Smad Smad4 dissociate intramolecular binding of Smad2/3 MH1 and MH2 domains. RI phosphorylation of Smad2/3 does all of these things. release Smad2/3 from the nucleus into the cytoplasm unmask the Smad2/3 nuclear localization signal (NLS).
If Sar1 is inserted into the ER membrane: O It is bound to GDP and recruits COPII coat proteins O It is not bound to any nucleotide O It is bound to GTP and recruits cargo O It is bound to GTP and recruits COPII coat proteins O It is bound to GTP and recruits clathrin coat proteins
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
The affinity of integrins for matrix components canbe modulated by changes to their cytoplasmic domains:a process known as inside-out signaling. You have iden-tified a key region in the cytoplasmic domains of αIIbβ3integrin that seems to be required for inside-out signaling(Figure Q19–3). Substitution of alanine for either D723in the β chain or R995 in the α chain leads to a high levelof spontaneous activation, under conditions where thewild-type chains are inactive. Your advisor suggests thatyou convert the aspartate in the β chain to an arginine(D723R) and the arginine in the α chain to an aspartate(R995D). You compare all three α chains (R995, R995A,and R995D) against all three β chains (D723, D723A, andD723R). You find that all pairs have a high level of sponta-neous activation, except D723 vs R995 (the wild type) andD723R vs R995D, which have low levels. Based on theseresults, how do you think the αIIbβ3 integrin is held in itsinactive state?
Match the primary sequence to its characteristics/function/fate v N-signal 1. mostly hydrophobic, interacts with SRP, cut off v signal-anchor 2. hydrophobic, interacts with SRP and translocon, becomes transmembrane helix v stop-anchor 3. found at carboxyl terminus of ER resident proteins, interaction with its receptor directs retrieval from Golgi v nuclear localization sequence 4. hydrophobic, interacts with translocon, becomes transmembrane helix v KDEL 5. basic, interacts with importin-alpha
Microtubules in an animal cell: O a. undergo assembly if the concentration of GTP-bound tubulin dimers is high and a cell is exposed to vinblastine O b. undergo disassembly if the concentration of GDP-bound tubulin dimers is high and a cell is exposed to taxol O c. undergo disassembly if the concentration of GTP-bound tubulin dimers is high and a cell is exposed to colchicine O d. undergo assembly if the concentration of GTP-bound tubulin dimers is high and a cell is exposed to colchicine
You are studying a cytoskeletal accessory protein, AB2. You believe it is involved in receptor-mediated endocytosis allowing for the entry of a novel virus, SARS-CoV X, into the host cell. To confirm that AB2 is required for viral entry, you engineer an AB2 protein containing an N-terminal hydrophobic signal sequence and a C-terminal KDEL sequence (AB2-SSKDEL) and express it in human epithelial airway cells. You compare cells expressing wild-type (WT) AB2 (lacking the signal sequence and KDEL sequence) with cells expressing AB2-SSKDEL. You are looking at the entry of a GFP (green) virus into cells. If AB2 is required for viral entry, via receptor-mediated endocytosis, what results would you expect to see in terms of viral entry? A. WT AB2 - Green ER AB2-SSKDEL - No green ER B. WT AB2-NO green cells AB2-SSKDEL - Many green cells OC. WT AB2 - Many green cells AB2-SSKDEL - NO green cells D.WT AB2 - Green nuclei AB2-SSKDEL - No green nuclei
A protein complex in the nucleus is responsible for transporting mRNA molecules into the cytoplasm. Describe the proteins that form this exporter. What two protein groups are probably behind the mechanism involved in the directional movement of the mRNP and exporter into the cytosol?

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