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9 Cards in this Set

  • Front
  • Back
Describe the ribosome.
2 subunits made of rRNA molecules and proteins.
Euk: 80 S; 60 + 40
rRNA functions: catalytic, H bonds to mRNA
protein function: promote binding of molecules
Describe the tRNA.
Made from a larger piece of precursor DNA that is cleaved. Usually modified to contain unusual bases
Has a cloverleaf structure
Describe charging/aminoacylation.
How amino acids are added to tRNAs.
1. Amino acid binds to enzyme and is coverted into active form through ATP hydrolysis -> becomes aminoacyladenic acid
2. AA transferred to 3' adenine end of tRNA
What are the 3 steps of Translation?
Initiation
Elongation
Termination
Describe Initiation.
Needs IFs to enhance binding proteins. IFs (1-3) bind to small su which can then bind to mRNA.
Shine-Delgarno sequence: base pairs with rRNA of small ribosomal su to make sure the start codon is in the correct position and aligns it correctly: Facilitates initiation.
Initiator tRNA carrying f-met binds to P site: IF-3 is released, large su binds to small su, GTP hydrolyzed, IF-1 and 2 are released. EF-Tu binds to tRNA allowing entry to the A site, anticodon bonds with mRNA codon, forming initiation complex.
Describe elongation.
3 sites: E, P (peptido, polypeptide is made), A (aminoacyl tRNA binds first)
The bond between aa and tRNA in P site is broken. At the same time ribosome catalyzes bond formation between f-met and 2nd aa (Now peptide attached to tRNA in A site)
Uncharged tRNA from P moves to E, then leaves ribosome complex. Entire complex shifts from A to P site.
Large subunite has a tunnel that allows the growing peptide chain to come out.
How is Ef-Tu restored?
wgaf
Describe termination.
Termination codon signals action of GTP-dependent factors to cleave peptide from last tRNA.
tRNA released, ribosome units disassemble.
Differences in euk. translation.
More complex. Initiation differs cuz mRNA has poly A tail and 5' cap. Only happens in cytoplasm. Small su scans mRNA till finds start codon in Kozak sequence, which allows binding.