Lecture 51-2 - Lecture 51: Translation II (protein...

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1 Lecture 51: Translation II (protein synthesis) and mapping structures Today’s lecture: Text pp. 1044-1058, 1101-1103, 1063-1067 Preprinted lecture notes 86-96, 136-138 Download from http://biochem.med.ufl.edu/coursetemp.php?cid=44 or http://www.mbi.ufl.edu/facilities/msg/bch4024-notes.html Assembling the components Regulating translation Looking at large assemblies DNA RNA Protein Replication Transcription Translation 1) mRNA is translated 5’ Æ 3’ 2) Polypeptide chain synthesis is amino (NH 3 + ) Æ carboxy (COO - ) 3) Three phases of the “ribosome cycle” a) Initiation: bind initiator tRNA……”AUG” b) Elongation: bind aa tRNA and form peptide bonds c) Termination Some general features of protein synthesis
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2 Protein synthesis requires energy 1) From ATP 1) Charging aatRNA 2) Eukaryotic initiation 2) From GTP 1) For binding tRNA to ribosome 1) At initiation 2) During elongation 2) For translocation of peptidyl tRNA and growing protein chain 3) For termination Estimated total (prokaryotes): 4 N ATP/GTP for a protein with N residues IF1 – promotes mRNA binding IF2 – initiator tRNA binding; binds GTP IF3 – Anti-association activity; promotes accurate start & mRNA binding Initiator tRNA binds at P site on 30S Shine-Dalgarno sequences position initiation codon in vicinity of decoding site, P site Chain initiation IF Initiation Factor protein Ribosome is “opened up” to allow positioning of mRNA strand A aminoacyl site P peptidyl site E exit site
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3 Note the first aaTRNA docks in the peptidyl site Chain initiation continued fMet N-formyl methionine
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Lecture 51-2 - Lecture 51: Translation II (protein...

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