Abstract:
:The translational GTPases promote initiation, elongation, and termination of protein synthesis by interacting with the ribosome. Mutations that impair GTP hydrolysis by eukaryotic translation initiation factor 5B/initiation factor 2 (eIF5B/IF2) impair yeast cell growth due to failure to dissociate from the ribosome following subunit joining. A mutation in helix h5 of the 18S rRNA in the 40S ribosomal subunit and intragenic mutations in domain II of eIF5B suppress the toxic effects associated with expression of the eIF5B-H480I GTPase-deficient mutant in yeast by lowering the ribosome binding affinity of eIF5B. Hydroxyl radical mapping experiments reveal that the domain II suppressors interface with the body of the 40S subunit in the vicinity of helix h5. As the helix h5 mutation also impairs elongation factor function, the rRNA and eIF5B suppressor mutations provide in vivo evidence supporting a functionally important docking of domain II of the translational GTPases on the body of the small ribosomal subunit.
journal_name
Mol Cell Bioljournal_title
Molecular and cellular biologyauthors
Shin BS,Kim JR,Acker MG,Maher KN,Lorsch JR,Dever TEdoi
10.1128/MCB.00896-08subject
Has Abstractpub_date
2009-02-01 00:00:00pages
808-21issue
3eissn
0270-7306issn
1098-5549pii
MCB.00896-08journal_volume
29pub_type
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