EF-G is a macromolecular mimic of EF-tu. It's role in translation is toTo cause the large subunit of the ribosome to disassociate with the small subunit of the ribosomeBind to the vacant A-site subsequent to peptide bond formation and resolve the hybrid state of theribosomeTo recruit the signal recognition particle (SRP) to the ribosome and to facilitate synthesis of membraneproteinsO To cause the large subunit to associate with the small subunit of the ribosomeShuttle an amino-acylated tRNA to the A site to initiate the peptidyl transfer reaction

Translation is the synthesis of the protein from m RNA. There are various initiation and elongation…

Answered: EF-G is a macromolecular mimic of…

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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Discuss the key factors & mechanisms during co-translational translocation by which START TRANSFER and STOP TRANSFER sequences help the protein generate appropriate number of transmembrane regions with N or C terminal on the designated side of the plasma membrane.(NO PLAGIARISM)
Explain why prokaryotic ribosomes can translate a circular mRNA molecule, whereas eukaryotic ribosomes normally cannot, even in the presence of the required cofactors.
During translation, the tRNA antlicodon sequence G-A-U vyould blnd to which MRNA codon (plck one of the cholces I -V below)? Note: all of the sequencos for tho quostlon and answors use the standard convention for representing ollgonuclootidos discussed In class whoro tho 5'-ond Is at the loft and the 3'-ond Is at the right. I) G-A-U II) U-A-G I) C-U-A IV) A-U-C V A-T-C OA. none of the cholces OB. IV Oc." OD.! OE, II
On average, how many phosphoanhydride bonds (P;-P; bonds) are directly hydrolyzed in thecourse of synthesizing a 200 amino acid protein? Assume that you begin with the mature mRNA,ribosomal subunits, tRNAs, free amino acids, and all necessary factors.
The cDNA sequence for a secreted protein shows that it contains two Asn-X-Ser/Thr motifs but nothing is known about the glycosylation of the protein. If you consider that either or both of these sites could be glycosylated and the oligosaccharides processed to either a Man5 high mannose structure or to a sialylated complex bi-antennary structure, how many possible glycoforms of the protein would there be? Explain why it is likely that such a protein would actually have very many more glycoforms.
Many blood clotting proteins undergo a post-translational modification in which specific glutamic acid residues (Glu) in the protein are converted to gamma-carboxyglutamic acid residues (Gla). See reaction scheme below. An example is the blood clotting protein Factor IX, which has 12 Glu in its N-terminus converted to Gla. This modification gives Factor IX the ability to bind calcium and phospholipid membranes. Bacteria do not have the enzyme required to convert Glu to Gla and therefore Factor IX proteins expressed in bacteria would not have the proper modifications. How might you engineer the translational apparatus of a bacterial cell line so that it produces Factor IX with Gla in the appropriate positions. How would you ensure that only the 12 Glu in Factor IX that are normally converted to Gla and not just all Glu (Limit 5-6 senetnces)?
In eukaryotic cells, secreted proteins are initially directed to the endoplasmic reticulum and then via the Golgi, where they are released into the extracellular environment through secretory vesicles. A more easier way would be for secretory protein-producing ribosomes to be localised to a translocon in the plasma membrane, with the protein being secreted directly during translation. Consider three possible benefits of the more roundabout method for protein secretion versus the simpler, more straightforward approach indicated.
Indicate (x) if the following statements about synthesis of proteins containing an ER signal sequence are True or False: True False i. Translation is initiated by ribosomes located on the ER membrane The signal recognition particle (SRP) binds a sequence of nonpolar (hydrophobic) amino acids. ii. iii. The ER signal sequence may be cleaved by signal peptidase on the cytoplasmic side of the ER membrane. iv. The part of a transmembrane protein that will ultimately be located outside of the cell is inserted into the lumen of the ER during translation. A stop transfer sequence is a series of polar amino acids that halts translocation of a newly synthesized peptide into the ER lumen.
Once the chains of peptides that make up lysyl-tRNA synthetase protein are synthesized in ribosomes, lysyl-tRNA synthetase needs to have the proper active site in order to perform its function, explain the process of protein folding necessary to have a proper 3-D structure, include effect of thermodynamics and different states in folding, including what happen when there are prolines that form peptide bonds with other amino acids, and any disulfide bridges
Predict the location(s) (intracellular or extracelular) and a brief description of WHY based on your knowledge of the transport processes in the following constructs. Assume a start codon is present and include any proteolytic processing that would be likely. 1. A PTS1 C-term peroxisomal targeting seq added to C term of a normally secreted protein with usual N -terminal signal sequence 2. Adding of N-terminal mitochondrial targeting sequence to protein with internal nuclear localization seq. 3. Adding N-terminal signal sequence of secreted protein to N-terminus a mitochondria matrix protein precursor with mitochondrial targeting sequence still present
What amino acid sequence does the following mRNA nucleotides sequence specify? 5'- AUGGCCAGCUGU -3' Express the sequence of amino axis's using the three-abbreviations, separate hyphens (e.g., Met-Ser-Thr-Lys-Gly).
Ribosomes markedly accelerate thehydrolysis of GTP bound to the complex of EF-Tu and aminoacyltRNA. What is the biological significance ofthis enhancement of GTPase activity by ribosomes?

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