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Effects of protein subunits removal on the computed motions of partial 30S structures of the ribosome.

ABSTRACT: The Anisotropic Network Model (ANM) is used to study motions of the 30S small ribosomal subunit. The effect of the absence of certain subunits on the motions of the remaining partial structures was investigated by removing one protein, pairs of proteins and selected sets of proteins at a time. Our results show that the removal of some proteins doesn't change the large-scale dynamics of the partial structures, but the removal of certain subunits does cause significant changes in motion of the remaining structure, and these changes can be reverted by the removal of other subunits, which indicates interdependence between motions of various parts of the 30S ribosomal structure. We further found that the subunits showing such interdependence have strong positive correlation of their motions, which indicates that these subunits function as a unit block in the 30S small ribosomal subunit. Dynamically interdependent subunit pairs identified in this paper are consistent with previous experimental observations that suggested dimerization of those subunits.

SUBMITTER: Yan A

PROVIDER: S-EPMC2665723 | biostudies-literature | 2008 Sep

REPOSITORIES: biostudies-literature

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Effects of protein subunits removal on the computed motions of partial 30S structures of the ribosome.

Yan Aimin A Wang Yongmei Y Kloczkowski Andrzej A Jernigan Robert L RL

Journal of chemical theory and computation 20080901 10

The Anisotropic Network Model (ANM) is used to study motions of the 30S small ribosomal subunit. The effect of the absence of certain subunits on the motions of the remaining partial structures was investigated by removing one protein, pairs of proteins and selected sets of proteins at a time. Our results show that the removal of some proteins doesn't change the large-scale dynamics of the partial structures, but the removal of certain subunits does cause significant changes in motion of the rem ...[more]

PMID: 19771145

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Project description:BackgroundYqeH, 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 findingsMnmE, another HAS-GTPase, but not circularly permuted, utilizes a potassium ion and water mediated interactions to drive GTP hydrolysis. Though the G-domain of MnmE and YqeH share only approximately 25% sequence identity, the conservation of characteristic sequence motifs between them prompted us to probe GTP hydrolysis machinery in YqeH, by employing homology modeling in conjunction with biochemical experiments. Here, we show that YqeH too, uses a potassium ion to drive GTP hydrolysis and stabilize the transition state. However, unlike MnmE, it does not dimerize in the transition state, suggesting alternative ways to stabilize switches I and II. Furthermore, we identify a potential catalytic residue in Asp-57, whose recognition, in the absence of structural information, was non-trivial due to the circular permutation in YqeH. Interestingly, when compared with MnmE, helix alpha2 that presents Asp-57 is relocated towards the N-terminus in YqeH. An analysis of the YqeH homology model, suggests that despite such relocation, Asp-57 may facilitate water mediated catalysis, similarly as the catalytic Glu-282 of MnmE. Indeed, an abolished catalysis by D57I mutant supports this inference.Conclusions/significanceAn uncommon means to achieve GTP hydrolysis utilizing a K(+) ion has so far been demonstrated only for MnmE. Here, we show that YqeH also utilizes a similar mechanism. While the catalytic machinery is similar in both, mechanistic differences may arise based on the way they are deployed. It appears that K(+) driven mechanism emerges as an alternative theme to stabilize the transition state and hydrolyze GTP in a subset of GTPases, such as the HAS-GTPases.

Dataset Information

Effects of protein subunits removal on the computed motions of partial 30S structures of the ribosome.

Publications

Effects of protein subunits removal on the computed motions of partial 30S structures of the ribosome.

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