Similarity and diversity of translational GTPase factors EF-G, EF4, and BipA: From structure to function

Ero, Rya; Kumar, Veerendra; Chen, Yun; Gao, Yong‐Gui

doi:10.1080/15476286.2016.1201627

Cited by 17 publications

(17 citation statements)

References 111 publications

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“…This prompts us to speculate that BipA is involved in other cellular functions as well as ribosome biogenesis. As a ribosome-associated GTPase, BipA shares several characteristic features with other trGTPases, such as LepA and EF-G (Ero et al, 2016). The primary and tertiary structures of BipA are highly similar with those of LepA and EF-G, and the enzymatic behaviors of BipA are the same as these proteins regarding GTP-dependent ribosome binding and ribosome-induced GTP hydrolysis.…”

Section: Discussionmentioning

confidence: 98%

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Elucidation of a Novel Role of YebC in Surface Polysaccharides Regulation of Escherichia coli bipA-Deletion

Choi

Jeon

et al. 2020

Front. Microbiol.

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Section: Discussionmentioning

confidence: 98%

“…The primary and tertiary structures of BipA are highly similar with those of LepA and EF-G, and the enzymatic behaviors of BipA are the same as these proteins regarding GTP-dependent ribosome binding and ribosome-induced GTP hydrolysis. Furthermore, the ribosomal binding sites of these three GTPases overlap (Ero et al, 2016).…”

Section: Discussionmentioning

confidence: 99%

Elucidation of a Novel Role of YebC in Surface Polysaccharides Regulation of Escherichia coli bipA-Deletion

Choi

Jeon

et al. 2020

Front. Microbiol.

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“…BipA is located in proximity to L6 (Fig. S5) (52), and LepA not only makes direct contact with L6, but also incorporates L10 and L12 ribosomal proteins via its nucleotide-independent chaperone activity (46,53). More recently, ⌬lepA strain was cold-sensitive and shown to accumulate the precursor 17S rRNA and 30S particles missing several ribosomal proteins, suggesting a novel 30S ribosome assembly GTPase (54).…”

Section: Discussionmentioning

confidence: 99%

“…BipA homologs share a structural similarity with trGTPases, such as IF2, EF-Tu, EF-G, LepA, and RF3 (46). These trGTPases possess a protein chaperone activity in their G-domains (47)(48)(49).…”

Section: Bipa Has a Chaperone-like Activity In Its G-domainmentioning

confidence: 99%

The GTPase BipA expressed at low temperature in Escherichia coli assists ribosome assembly and has chaperone-like activity

Choi

Hwang

2018

Journal of Biological Chemistry

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Edited by Ronald C. Wek BPI-inducible protein A (BipA) is a conserved ribosome-associated GTPase in bacteria that is structurally similar to other GTPases associated with protein translation, including IF2, EF-Tu, and EF-G. Its binding site on the ribosome appears to overlap those of these translational GTPases. Mutations in the bipA gene cause a variety of phenotypes, including cold and antibiotics sensitivities and decreased pathogenicity, implying that BipA may participate in diverse cellular processes by regulating translation. According to recent studies, a bipA-deletion strain of Escherichia coli displays a ribosome assembly defect at low temperature, suggesting that BipA might be involved in ribosome assembly. To further investigate BipA's role in ribosome biogenesis, here, we compared and analyzed the ribosomal protein compositions of MG1655 WT and bipA-deletion strains at 20°C. Aberrant 50S ribosomal subunits (i.e. 44S particles) accumulated in the bipA-deletion strain at 20°C, and the ribosomal protein L6 was absent in these 44S particles. Furthermore, bipA expression was significantly stimulated at 20°C, suggesting that it encodes a cold shock-inducible GTPase. Moreover, the transcriptional regulator cAMP receptor protein (CRP) positively promoted bipA expression only at 20°C. Importantly, GFP and ␣-glucosidase refolding assays revealed that BipA has chaperone activity. Our findings indicate that BipA is a cold shock-inducible GTPase that participates in 50S ribosomal subunit assembly by incorporating the L6 ribosomal protein into the 44S particle during the assembly.

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“…Another functional aspect of BipA is that it can associate with the ribosome and shares structural similarity with translational GTPases (trGTPases) including IF2, EF-G, EF-Tu, and LepA (Ero et al, 2016). EF-G is arranged with domains G, G , II, III, IV, and V (AEevarsson et al, 1994;Czworkowski et al, 1994), and all of the above-mentioned trGTPases contain domains G and II.…”

Section: Introductionmentioning

confidence: 99%

Overexpressed L20 Rescues 50S Ribosomal Subunit Assembly Defects of bipA-Deletion in Escherichia coli

Choi

Jeon

et al. 2020

Front. Microbiol.

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The BipA (BPI-inducible protein A) protein is highly conserved in a large variety of bacteria and belongs to the translational GTPases, based on sequential and structural similarities. Despite its conservation in bacteria, bipA is not essential for cell growth under normal growth conditions. However, at 20 • C, deletion of bipA causes not only severe growth defects but also several phenotypic changes such as capsule production, motility, and ribosome assembly, indicating that it has global regulatory properties. Our recent studies revealed that BipA is a novel ribosome-associating GTPase, whose expression is cold-shock-inducible and involved in the incorporation of the ribosomal protein (r-protein) L6. However, the precise mechanism of BipA in 50S ribosomal subunit assembly is not completely understood. In this study, to demonstrate the role of BipA in the 50S ribosomal subunit and possibly to find an interplaying partner(s), a genomic library was constructed and suppressor screening was conducted. Through screening, we found a suppressor gene, rplT, encoding r-protein L20, which is assembled at the early stage of ribosome assembly and negatively regulates its own expression at the translational level. We demonstrated that the exogenous expression of rplT restored the growth of bipA-deleted strain at low temperature by partially recovering the defects in ribosomal RNA processing and ribosome assembly. Our findings suggest that the function of BipA is pivotal for 50S ribosomal subunit biogenesis at a low temperature and imply that BipA and L20 may exert coordinated actions for proper ribosome assembly under cold-shock conditions.

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Similarity and diversity of translational GTPase factors EF-G, EF4, and BipA: From structure to function

Cited by 17 publications

References 111 publications

Elucidation of a Novel Role of YebC in Surface Polysaccharides Regulation of Escherichia coli bipA-Deletion

Elucidation of a Novel Role of YebC in Surface Polysaccharides Regulation of Escherichia coli bipA-Deletion

The GTPase BipA expressed at low temperature in Escherichia coli assists ribosome assembly and has chaperone-like activity

Overexpressed L20 Rescues 50S Ribosomal Subunit Assembly Defects of bipA-Deletion in Escherichia coli

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