Related ArticlesDetermination of the pKa of the N-terminal amino group of ubiquitin by NMR.
Sci Rep. 2017 Mar 02;7:43748
Authors: Oregioni A, Stieglitz B, Kelly G, Rittinger K, Frenkiel T
Abstract
Ubiquitination regulates nearly every aspect of cellular life. It is catalysed by a cascade of three enzymes and results in the attachment of the C-terminal carboxylate of ubiquitin to a lysine side chain in the protein substrate. Chain extension occurs via addition of subsequent ubiquitin molecules to either one of the seven lysine residues of ubiquitin, or via its N-terminal ?-amino group to build linear ubiquitin chains. The pKa of lysine side chains is around 10.5 and hence E3 ligases require a mechanism to deprotonate the amino group at physiological pH to produce an effective nucleophile. In contrast, the pKa of N-terminal ?-amino groups of proteins can vary significantly, with reported values between 6.8 and 9.1, raising the possibility that linear chain synthesis may not require a general base. In this study we use NMR spectroscopy to determine the pKa for the N-terminal ?-amino group of methionine1 of ubiquitin for the first time. We show that it is 9.14, one of the highest pKa values ever reported for this amino group, providing a rational for the observed need for a general base in the E3 ligase HOIP, which synthesizes linear ubiquitin chains.
[NMR paper] The N-terminal ubiquitin-binding region of ubiquitin-specific protease 28 modulates its deubiquitination function: NMR structural and mechanistic insights.
The N-terminal ubiquitin-binding region of ubiquitin-specific protease 28 modulates its deubiquitination function: NMR structural and mechanistic insights.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-highwire.gif Related Articles The N-terminal ubiquitin-binding region of ubiquitin-specific protease 28 modulates its deubiquitination function: NMR structural and mechanistic insights.
Biochem J. 2015 Oct 15;471(2):155-65
Authors: Wen Y, Shi L, Ding Y, Cui R, He WT, Hu HY,...
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NMR Structure of the C-Terminal Domain of a Tyrosyl-tRNA Synthetase That Functions in Group I Intron Splicing
NMR Structure of the C-Terminal Domain of a Tyrosyl-tRNA Synthetase That Functions in Group I Intron Splicing
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi200189u/aop/images/medium/bi-2011-00189u_0010.gif
Biochemistry
DOI: 10.1021/bi200189u
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NMR structure of the C-terminal domain of a tyrosyl-tRNA synthetase that functions in group I intron splicing.
NMR structure of the C-terminal domain of a tyrosyl-tRNA synthetase that functions in group I intron splicing.
NMR structure of the C-terminal domain of a tyrosyl-tRNA synthetase that functions in group I intron splicing.
Biochemistry. 2011 Mar 25;
Authors: Paukstelis PJ, Chari N, Lambowitz AM, Hoffman DW
The mitochondrial tyrosyl-tRNA synthetases (mt TyrRSs) of Pezizomycotina fungi are bifunctional proteins that aminoacylate mitochondrial tRNATyr and are structure-stabilizing splicing cofactors for group I introns. Studies with the Neurospora...
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[NMR paper] NMR structure of the amino-terminal domain from the Tfb1 subunit of TFIIH and charact
NMR structure of the amino-terminal domain from the Tfb1 subunit of TFIIH and characterization of its phosphoinositide and VP16 binding sites.
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Biochemistry. 2005 May 31;44(21):7678-86
Authors: Di Lello P, Nguyen BD, Jones TN, Potempa K, Kobor MS, Legault P, Omichinski JG
General transcription factor IIH (TFIIH) is recruited to the preinitiation complex (PIC) through direct interactions...
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[NMR paper] Involvement of various amino- and carboxyl-terminal residues in the active site of th
Involvement of various amino- and carboxyl-terminal residues in the active site of the histidine-containing protein HPr of the phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus carnosus: site-directed mutagenesis with the ptsH gene, biochemical characterization and NMR studies of the mutant proteins.
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[NMR paper] Complete 15N and 1H NMR assignments for the amino-terminal domain of the phage 434 re
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http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Complete 15N and 1H NMR assignments for the amino-terminal domain of the phage 434 repressor in the urea-unfolded form.
Proc Natl Acad Sci U S A. 1992 May 15;89(10):4397-401
Authors: Neri D, Wider G, Wüthrich K
The amino-terminal domain of the phage 434 repressor consisting of residues 1-69...
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[NMR paper] 1H-NMR investigation of the interaction of the amino terminal domain of the LexA repr
1H-NMR investigation of the interaction of the amino terminal domain of the LexA repressor with a synthetic half-operator.
Related Articles 1H-NMR investigation of the interaction of the amino terminal domain of the LexA repressor with a synthetic half-operator.
J Biomol Struct Dyn. 1991 Dec;9(3):447-61
Authors: Ottleben G, Messori L, Rüterjans H, Kaptein R, Granger-Schnarr M, Schnarr M
A synthetic half-operator DNA-duplex, d(GCTACTGTATGT), containing a portion of the proposed recognition sequence (CTGT) of several "SOS" genes, has been...
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[NMR paper] 1H-NMR investigation of the interaction of the amino terminal domain of the LexA repr
1H-NMR investigation of the interaction of the amino terminal domain of the LexA repressor with a synthetic half-operator.
Related Articles 1H-NMR investigation of the interaction of the amino terminal domain of the LexA repressor with a synthetic half-operator.
J Biomol Struct Dyn. 1991 Dec;9(3):447-61
Authors: Ottleben G, Messori L, Rüterjans H, Kaptein R, Granger-Schnarr M, Schnarr M
A synthetic half-operator DNA-duplex, d(GCTACTGTATGT), containing a portion of the proposed recognition sequence (CTGT) of several "SOS" genes, has been...
Determination of the pKa of the N-terminal amino group of ubiquitin by NMR.
Linear Mode
