Protein biosynthesis: aminoacyl-tRNA synthetases and aminoacylation

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Recognition of tRNAs by AspRS (class II) and ArgRS (class I), shown as outlines. The tRNAAsp shown will bind to either. Sites on the opposite sides of tRNA make contacts with the two AaRSs (blue balls - contacts with AspRS, yellow balls - with ArgRS).
Class I aaRSs interact with the 5’ nucleotides of the acceptor stem and class II aaRSs with the 3’ nucleotides. The CCA arm of tRNA adopts different conformations in complexes with the class I and class II AaRSs.
Page 1: Protein biosynthesis: aminoacyl-tRN
Page 4 and 5: Comparison of class I and class II
Page 6 and 7: Evolution and sub-groups of AaRS
Page 8 and 9: Class II active site, 3 conserved m
Page 13 and 14: The structure of the complex betwee
Page 16 and 17: LysRS of most eukaryotes and bacter
Page 19 and 20: • inhibiors of AaRSs can be used
Page 21: tRNA
Page 24: Sequence elements: Mostly non-modif
Page 27 and 28: Structural elements: identity eleme
Page 29 and 30: • Anti-determinants: negative sig
Page 31: • identity elements mostly cluste
Page 34: Step 1 - activation of amino acid a
Page 37 and 38: adenosine P P P + ATP Step 1 O C O
Page 39 and 40: Structure of the large fragment of
Page 41 and 42: Accuracy of aminoacylation Accurate
Page 44 and 45: • AaRS have difficulties discrimi
Page 46 and 47: tRNA editing Some AaRSs remove thei
Page 48 and 49: The flexible CCA arm of an aminoacy
Page 51 and 52: • Val is rejected based on chemic
Page 53 and 54: 2. When GlnRS is missing (B. subtil
Page 55: 3. When AsnRS is missing (in T. the
Page 61 and 62:
5. Selenosysteine - the 21-st amino
Page 63 and 64:
6. Initiator fMettRNA is formylated
Page 66:
Additional reading: 1. TiBS, July 2
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Protein biosynthesis: aminoacyl-tRNA synthetases and aminoacylation

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