Which of the following is the most likely reason that many ribosomes do not attach to the surface of the rough endoplasmic reticulum during translation?
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- After isolating the rough endoplasmic reticulum from the rest of the cytoplasm, you purify the RNAs attached to it. Which of the following proteins do you not expect to be translated from the RNAs associated with the rough endoplasmic reticulum? Lysosomal enzymes Plasma membrane proteins Extracellular matrix proteins Golgi enzymes Peroxisomal proteinsWhich of the following statements is CORRECT for a protein with an N-terminal ER signal sequence? O During translation, the ER signal sequence directly inserts into the membrane before import into the ER. O The protein is fully synthesized in the cytosol and then taken to the translocon for import into the ER. The SRP, SRP receptor and translocon form a complex and bind a ribosome before translation. O SRP binds the ER signal sequence and the SRP receptor during translation.gene normally contains an N' terminal ER signal sequence and an internal stop transfer sequence. The ER signal sequence is recognized and used during the protein trafficking process, as normal. After translation is completed a signal peptidase enzyme cleaves the N' ER signal sequence but the internal sequence is not cleaved. Which of the following figures best represents the orientation of the protein product after translation? N Extracellular Extracellular Extracellular Extracellular -N' C' N Lumen Lumen Lumen Lumen N' A В C
- Ribosomes that do not anchor on the surface of the rough endoplasmic reticulum during translation are most likely synthesizing Golgi proteins. synthesizing cytoplasmic proteins. synthesizing lysosomal proteins. synthesizing ER proteins.There are two ways in which rearrangement of domain- encoding gene segments can result in novel protein functions. Which of the following is NOT included? Domain shuffling Domain duplication Domain replication Domain substitution Which of the following features are NOT shared by prokaryotic and eukaryotic cells? shared metabolic pathways similar mechanism for synthesizing and inserting membrane proteins plasma membrane of similar structure nucleosomes of similar constructionPart A Shown above is a schematic diagram of the E. coli leader peptidase (Lep) which has several basic amino acids in a cytoplasmic loop. Propose a mutant of Lep that would be a test of the "inside positive" rule for the orientation of proteins in membranes. Match the words in the left column to the appropriate blanks in the sentences on the right. Make certain each sentence is complete before submitting your answer. terminal reversed same (+) (-) center 1. Make mutant Lep that substitutes noncharged residues for the chains in the loop, and put charged side chains in 2. If the inside-positive rule applies, the mutant ought to have the membrane. Reset Help charged side positions. orientation in the
- Please draw or trace a pathway of any protein from translation to the plasma membrane. Name the protein (make sure it is a transemembrane protein). The protein in question must also have seceral protein modifications including, but not limited to, N-linked glycosylation, cysteine disulfide bonds, lipid modifications, and 3-D foldingWhat distinguishes proteins that will be released into the cytoplasm after translation from proteins that will be released into the rough ER after translation? whether they are synthesized by small or large ribosomal subunits whether they will be enzymes or structural proteins presence of a signal sequence on the protein number of start codons on their mRNAs how hydrophobic the proteins areAntibiotic X binds to the 50S ribosomal subunit of 70S ribosomes and blocks normal ribosomal function. Which of the following is true of this drug? It would interfere with protein synthesis in bacteria, but not affect eukaryotic ribosomes. It would interfere with peptidoglycan syntheis/repair in bacteria, but not affect eukaryotes as they lack peptidoglycan. It would interfere with mRNA transcription in bacteria and in eukaryotes. It would interfere with protein synthesis in bacteria and eukaryotes. It would interfere with mRNA transcription in bacteria, but not affect eukaryotic transcription. It would interfere with peptidoglycan syntheis/repair in bacteria, as well as in eukaryotes that possess cell walls.
- Which of the following is the first step of translation in a eukaryotic cell? O a RNA containing activated methionine binds to AUG of the messenger RNA the ribosome reaches a stop codon the small subunit of the ribosome recognizes and attaches to the 5' cap of mRNA O binding of the larger ribosomal subunit to smaller ribosomal subunitsPlace the steps below in the correct order to accurately reflect the steps by which a secretory protein is co-translationally imported into the lumen of the endoplasmic reticulum: As the polypeptide elongates and translocates into the ER, the signal peptidase cleaves the signal peptide. The SRP binds the SRP receptor, directing the ribosome to dock on the ER membrane. Termination of translation, results in the release of the polypeptide into the ER lumen, release of the ribosome from the ER membrane, and closing of the channel. The signal recognition particle (SRP) binds to the signal sequence on a newly synthesized polypeptide and stalls translation. The channel in the ER membrane opens and the polypeptide is inserted into the ER lumen. The SRP is released. A.6-4-2-3-1-5 B.4-2-5-1-3-6 C.3-1-6-2-4-5 D.1-2-3-4-5-6 E.2-6-1-5-4-3A 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?