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YsxC is an essential P-loop GTPase that interacts with the 50S subunit of the ribosome. The putative implication in ribosome binding of two basic clusters of YsxC, a conserved positively charged patch including R31, R116, H117 and K146 lying adjacent to the nucleotide-binding site, and the C-terminal alpha helix, was investigated. C-terminal truncation variants of YsxC were unable to bind to both ribosome and rRNAs, whereas mutations in the other cluster did not affect YsxC binding. Our results indicate that the basic C-terminal region of YsxC is required for its binding to the 50S ribosomal subunit.

Titel:	The C-terminal α-helix of YsxC is essential for its binding to 50S ribosome and rRNAs.
Autor/in / Beteiligte Person:	Wicker-Planquart, C ; Ceres, N ; Jault, JM
Zeitschrift:	FEBS letters, Jg. 589 (2015-07-22), Heft 16, S. 2080-6
Veröffentlichung:	Jan. 2016- : West Sussex : John Wiley & Sons Ltd. ; <i>Original Publication</i>: Amsterdam, North-Holland on behalf of the Federation of European Biochemical Societies., 2015
Medientyp:	academicJournal
ISSN:	1873-3468 (electronic)
DOI:	10.1016/j.febslet.2015.06.006
Schlagwort:	Amino Acid Substitution Arginine chemistry Bacillus subtilis metabolism Bacterial Proteins chemistry Bacterial Proteins genetics Binding Sites GTP Phosphohydrolases chemistry GTP Phosphohydrolases genetics Histidine chemistry Hot Temperature Ligands Lysine chemistry Molecular Conformation Molecular Dynamics Simulation Mutant Proteins chemistry Mutant Proteins metabolism Peptide Fragments chemistry Peptide Fragments genetics Peptide Fragments metabolism Protein Stability RNA, Bacterial chemistry RNA, Bacterial metabolism RNA, Ribosomal, 16S chemistry RNA, Ribosomal, 23S chemistry Recombinant Proteins chemistry Recombinant Proteins metabolism Ribosome Subunits, Large, Bacterial chemistry Ribosome Subunits, Small, Bacterial chemistry Ribosome Subunits, Small, Bacterial metabolism Bacillus subtilis enzymology Bacterial Proteins metabolism GTP Phosphohydrolases metabolism Models, Molecular RNA, Ribosomal, 16S metabolism RNA, Ribosomal, 23S metabolism Ribosome Subunits, Large, Bacterial metabolism
Sonstiges:	Nachgewiesen in: MEDLINE Sprachen: English Publication Type: Journal Article; Research Support, Non-U.S. Gov't Language: English [FEBS Lett] 2015 Jul 22; Vol. 589 (16), pp. 2080-6. <i>Date of Electronic Publication: </i>2015 Jun 21. MeSH Terms: Models, Molecular* ; Bacillus subtilis / enzymology ; Bacterial Proteins / metabolism ; GTP Phosphohydrolases / metabolism ; RNA, Ribosomal, 16S / metabolism ; RNA, Ribosomal, 23S / metabolism ; Ribosome Subunits, Large, Bacterial / metabolism ; Amino Acid Substitution ; Arginine / chemistry ; Bacillus subtilis / metabolism ; Bacterial Proteins / chemistry ; Bacterial Proteins / genetics ; Binding Sites ; GTP Phosphohydrolases / chemistry ; GTP Phosphohydrolases / genetics ; Histidine / chemistry ; Hot Temperature ; Ligands ; Lysine / chemistry ; Molecular Conformation ; Molecular Dynamics Simulation ; Mutant Proteins / chemistry ; Mutant Proteins / metabolism ; Peptide Fragments / chemistry ; Peptide Fragments / genetics ; Peptide Fragments / metabolism ; Protein Stability ; RNA, Bacterial / chemistry ; RNA, Bacterial / metabolism ; RNA, Ribosomal, 16S / chemistry ; RNA, Ribosomal, 23S / chemistry ; Recombinant Proteins / chemistry ; Recombinant Proteins / metabolism ; Ribosome Subunits, Large, Bacterial / chemistry ; Ribosome Subunits, Small, Bacterial / chemistry ; Ribosome Subunits, Small, Bacterial / metabolism Contributed Indexing: Keywords: Bacillus subtilis; GTPase; Ribosome binding; YsxC Substance Nomenclature: 0 (Bacterial Proteins) ; 0 (Ligands) ; 0 (Mutant Proteins) ; 0 (Peptide Fragments) ; 0 (RNA, Bacterial) ; 0 (RNA, Ribosomal, 16S) ; 0 (RNA, Ribosomal, 23S) ; 0 (Recombinant Proteins) ; 4QD397987E (Histidine) ; 94ZLA3W45F (Arginine) ; EC 3.6.1.- (GTP Phosphohydrolases) ; K3Z4F929H6 (Lysine) Entry Date(s): Date Created: 20150624 Date Completed: 20151012 Latest Revision: 20150722 Update Code: 20240513

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The C-terminal α-helix of YsxC is essential for its binding to 50S ribosome and rRNAs.