Unknown

Dataset Information

0

Roles of elusive translational GTPases come to light and inform on the process of ribosome biogenesis in bacteria.


ABSTRACT: Protein synthesis relies on several translational GTPases (trGTPases), related proteins that couple the hydrolysis of GTP to specific molecular events on the ribosome. Most bacterial trGTPases, including IF2, EF-Tu, EF-G and RF3, play well-known roles in translation. The cellular functions of LepA (also termed EF4) and BipA (also termed TypA), conversely, have remained enigmatic. Recent studies provide compelling in vivo evidence that LepA and BipA function in biogenesis of the 30S and 50S subunit respectively. These findings have important implications for ribosome biogenesis in bacteria. Because the GTPase activity of each of these proteins depends on interactions with both ribosomal subunits, some portion of 30S and 50S assembly must occur in the context of the 70S ribosome. In this review, we introduce the trGTPases of bacteria, describe the new functional data on LepA and BipA, and discuss the how these findings shape our current view of ribosome biogenesis in bacteria.

SUBMITTER: Gibbs MR 

PROVIDER: S-EPMC5796857 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

Roles of elusive translational GTPases come to light and inform on the process of ribosome biogenesis in bacteria.

Gibbs Michelle R MR   Fredrick Kurt K  

Molecular microbiology 20171229 4


Protein synthesis relies on several translational GTPases (trGTPases), related proteins that couple the hydrolysis of GTP to specific molecular events on the ribosome. Most bacterial trGTPases, including IF2, EF-Tu, EF-G and RF3, play well-known roles in translation. The cellular functions of LepA (also termed EF4) and BipA (also termed TypA), conversely, have remained enigmatic. Recent studies provide compelling in vivo evidence that LepA and BipA function in biogenesis of the 30S and 50S subun  ...[more]

Similar Datasets

| S-EPMC4895721 | biostudies-literature
| S-EPMC1780047 | biostudies-literature
| S-EPMC1489179 | biostudies-literature
2017-02-08 | PXD004074 | Pride
| S-EPMC5084732 | biostudies-literature
| S-EPMC4835026 | biostudies-literature
| S-EPMC3907300 | biostudies-literature
2016-01-13 | E-GEOD-72899 | biostudies-arrayexpress
2016-01-13 | GSE72899 | GEO
| S-EPMC4835038 | biostudies-literature