Related ArticlesBackbone and sidechain NMR assignments for the ribosome maturation factor RimP from Escherichia coli.
Biomol NMR Assign. 2020 Apr 17;:
Authors: Schedlbauer A, Ochoa-Lizarralde B, Iturrioz I, Çapuni R, Diercks T, de Astigarraga E, Fucini P, Connell SR
Abstract
Ribosome biogenesis is an energetically expensive and complex cellular process that involves the coordinated folding of the ribosomal RNA and dozens of ribosomal proteins. It proceeds along multiple parallel pathways and is guided by trans-acting factors called ribosome assembly factors. Although this process has been studied for decades, there are still many open questions regarding the role of the ribosome assembly factors in directing the folding of ribosome biogenesis intermediates. RimP is one of the early acting factors and guides the assembly of the small 30S ribosomal subunit by facilitating the binding of ribosomal proteins uS5 and uS12. Here we report the virtually complete 1H, 15N, and 13C chemical shift assignment of RimP from Escherichia coli. The NMR chemical shift data, deposited in the BMRB data bank under Accession No. 28014, indicates a widely folded protein composed of three alpha helices and eight beta strands.
PMID: 32303998 [PubMed - as supplied by publisher]
[NMR paper] Backbone and side-chain (1)H, (13)C, and (15)N NMR assignments of the N-terminal domain of Escherichia coli LpoA.
Backbone and side-chain (1)H, (13)C, and (15)N NMR assignments of the N-terminal domain of Escherichia coli LpoA.
Related Articles Backbone and side-chain (1)H, (13)C, and (15)N NMR assignments of the N-terminal domain of Escherichia coli LpoA.
Biomol NMR Assign. 2014 Feb 4;
Authors: Jean NL, Bougault C, Derouaux A, Callens G, Vollmer W, Simorre JP
Abstract
The peptidoglycan is a major component of the bacterial cell wall and is essential to maintain cellular integrity and cell shape. Penicillin-Binding Proteins (PBPs) catalyze the final...
nmrlearner
Journal club
0
02-05-2014 06:08 PM
[NMR paper] Backbone and side chain NMR assignments for the ribosome assembly factor Nop6 from Saccharomyces cerevisiae.
Backbone and side chain NMR assignments for the ribosome assembly factor Nop6 from Saccharomyces cerevisiae.
Backbone and side chain NMR assignments for the ribosome assembly factor Nop6 from Saccharomyces cerevisiae.
Biomol NMR Assign. 2013 Aug 7;
Authors: Wurm JP, Lioutikov A, Kötter P, Entian KD, Wöhnert J
Abstract
The Saccharomyces cerevisiae Nop6 protein is involved in the maturation of the small ribosomal subunit. It contains a central RNA binding domain and a predicted C-terminal coiled-coil domain. Here we report the almost...
nmrlearner
Journal club
0
08-08-2013 03:46 PM
Backbone and side chain NMR resonance assignments for an archaeal homolog of the endonuclease Nob1 involved in ribosome biogenesis.
Backbone and side chain NMR resonance assignments for an archaeal homolog of the endonuclease Nob1 involved in ribosome biogenesis.
Backbone and side chain NMR resonance assignments for an archaeal homolog of the endonuclease Nob1 involved in ribosome biogenesis.
Biomol NMR Assign. 2011 Jul 6;
Authors: Veith T, Wurm JP, Duchardt-Ferner E, Weis B, Martin R, Safferthal C, Bohnsack MT, Schleiff E, Wöhnert J
Eukaryotic ribosome biogenesis requires the concerted action of ~200 auxiliary protein factors on the nascent ribosome. For many of these...
nmrlearner
Journal club
0
07-07-2011 05:12 PM
(1)H, (13)C and (15)N NMR assignments of the Escherichia coli Orf135 protein.
(1)H, (13)C and (15)N NMR assignments of the Escherichia coli Orf135 protein.
(1)H, (13)C and (15)N NMR assignments of the Escherichia coli Orf135 protein.
Biomol NMR Assign. 2011 May 7;
Authors: Kawasaki K, Yoneyama M, Murata-Kamiya N, Harashima H, Kojima C, Ito Y, Kamiya H, Mishima M
Escherichia coli Orf135 protein is thought to be an enzyme that efficiently hydrolyzes oxidatively damaged nucleotides such as 2-hydroxy-dATP, 8-hydroxy-dGTP and 5-hydroxy-CTP, in addition to 5-methyl-dCTP, dCTP and CTP, thus preventing mutations in cells caused by...
nmrlearner
Journal club
0
05-10-2011 05:11 PM
[NMR paper] NMR assignments of the cold-shock protein ribosome-binding factor A (RbfA) from Therm
NMR assignments of the cold-shock protein ribosome-binding factor A (RbfA) from Thermotoga maritima.
Related Articles NMR assignments of the cold-shock protein ribosome-binding factor A (RbfA) from Thermotoga maritima.
J Biomol NMR. 2005 Jan;31(1):73-4
Authors: Grimm SK, Wöhnert J
nmrlearner
Journal club
0
11-24-2010 11:14 PM
[NMR paper] Backbone assignments and secondary structure of the Escherichia coli enzyme-II mannit
Backbone assignments and secondary structure of the Escherichia coli enzyme-II mannitol A domain determined by heteronuclear three-dimensional NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Backbone assignments and secondary structure of the Escherichia coli enzyme-II mannitol A domain determined by heteronuclear three-dimensional...
nmrlearner
Journal club
0
08-22-2010 03:01 AM
[NMR paper] NMR study of the phosphate-binding elements of Escherichia coli elongation factor Tu
NMR study of the phosphate-binding elements of Escherichia coli elongation factor Tu catalytic domain.
Related Articles NMR study of the phosphate-binding elements of Escherichia coli elongation factor Tu catalytic domain.
Biochemistry. 1991 Nov 12;30(45):10872-7
Authors: Lowry DF, Cool RH, Redfield AG, Parmeggiani A
The phosphoryl-binding elements in the GDP-binding domain of elongation factor Tu were studied by heteronuclear proton observe methods. Five proton resonances were found below 10.5 ppm. Two of these were assigned to the amide...
nmrlearner
Journal club
0
08-21-2010 11:12 PM
[NMR paper] NMR study of the phosphate-binding elements of Escherichia coli elongation factor Tu
NMR study of the phosphate-binding elements of Escherichia coli elongation factor Tu catalytic domain.
Related Articles NMR study of the phosphate-binding elements of Escherichia coli elongation factor Tu catalytic domain.
Biochemistry. 1991 Nov 12;30(45):10872-7
Authors: Lowry DF, Cool RH, Redfield AG, Parmeggiani A
The phosphoryl-binding elements in the GDP-binding domain of elongation factor Tu were studied by heteronuclear proton observe methods. Five proton resonances were found below 10.5 ppm. Two of these were assigned to the amide...
Backbone and sidechain NMR assignments for the ribosome maturation factor RimP from Escherichia coli.
Linear Mode
