Deciphering the catalytic machinery in 30S ribosome assembly GTPase YqeH.

ABSTRACT:

Background

YqeH, a circularly permuted GTPase (cpGTPase), which is conserved across bacteria and eukaryotes including humans is important for the maturation of small (30S) ribosomal subunit in Bacillus subtilis. Recently, we have shown that it binds 30S in a GTP/GDP dependent fashion. However, the catalytic machinery employed to hydrolyze GTP is not recognized for any of the cpGTPases, including YqeH. This is because they possess a hydrophobic substitution in place of a catalytic glutamine (present in Ras-like GTPases). Such GTPases were categorized as HAS-GTPases and were proposed to follow a catalytic mechanism, different from the Ras-like proteins.

Methodology/principal findings

MnmE, another HAS-GTPase, but not circularly permuted, utilizes a potassium ion and water medi

SUBMITTER: Anand B 

PROVIDER: S-EPMC2848588 | biostudies-literature | 2010 Apr

REPOSITORIES: biostudies-literature