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Article: Backbone and side-chain 1H, 15N and 13C resonance assignments of S18Y mutant of ubiquitin carboxy-terminal hydrolase L1

TitleBackbone and side-chain 1H, 15N and 13C resonance assignments of S18Y mutant of ubiquitin carboxy-terminal hydrolase L1
Authors
KeywordsNMR spectroscopy
Parkinson's disease
Resonance assignment
Ubiquitin
Ubiquitin carboxy-terminal hydrolase L1
Issue Date2011
PublisherSpringer Netherlands. The Journal's web site is located at http://www.springer.com/physics/biophysics/journal/12104
Citation
Biomolecular Nmr Assignments, 2011, v. 5 n. 2, p. 165-168 How to Cite?
AbstractUbiquitin carboxy-terminal hydrolase L1 (UCH-L1), also known as PGP9.5, is a protein of 223 amino acids. Although it was originally characterized as a deubiquitinating enzyme, recent studies indicate that it also functions as a ubiquitin (Ub) ligase and a mono-Ub stabilizer. It is highly abundant in brain, constituting up to 2% of total brain proteins. Down-regulation and extensive oxidative modification of UCH-L1 have been observed in the brains of Alzheimer's disease (AD) and Parkinson's disease (PD) patients. Mutations in the UCH-L1 gene have been reported to be linked to Parkinson's disease, in particular, the I93 M variant is associated with a higher susceptibility of PD in contrast to a higher protection against PD for the S18Y variant. Hence, the structure of UCH-L1 and the underlying effects of disease associated mutations on the structure and function of UCH-L1 are of considerable interest. Here, we report the NMR spectral assignments of the S18Y human UCH-L1 mutant with the aim to obtain better understanding about the risk of Parkinson's disease against structural and dynamical changes induced by this mutation on UCH-L1. © 2011 The Author(s).
Persistent Identifierhttp://hdl.handle.net/10722/144868
ISSN
2015 Impact Factor: 0.687
2015 SCImago Journal Rankings: 0.325
PubMed Central ID
ISI Accession Number ID
Funding AgencyGrant Number
Research Grants Council of Hong KongGRF 7755/08 M
7765/09 M
Funding Information:

This work was supported by the Research Grants Council of Hong Kong (GRF 7755/08 M, 7765/09 M)

References

Naito S, Mochizuki H, Yasuda T et al (2006) Characterization of multimetric variants of ubiquitin carboxyl-terminal hydrolase L1 in water by small-angle neutron scattering. Biochem Biophys Res Commun 339:717–725 doi: 10.1016/j.bbrc.2005.11.066

Osaka H, Wang YL, Takada K et al (2003) Ubiquitin carboxy-terminal hydrolase L1 binds to and stabilizes monoubiquitin in neuron. Hum Mol Genet 12:1945–1958 doi: 10.1093/hmg/ddg211

Wishart DS, Sykes BD (1994) The13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR 4:171–180 doi: 10.1007/BF00175245

 

DC FieldValueLanguage
dc.contributor.authorTse, HSen_HK
dc.contributor.authorHu, HYen_HK
dc.contributor.authorSze, KHen_HK
dc.date.accessioned2012-02-21T05:44:38Z-
dc.date.available2012-02-21T05:44:38Z-
dc.date.issued2011en_HK
dc.identifier.citationBiomolecular Nmr Assignments, 2011, v. 5 n. 2, p. 165-168en_HK
dc.identifier.issn1874-2718en_HK
dc.identifier.urihttp://hdl.handle.net/10722/144868-
dc.description.abstractUbiquitin carboxy-terminal hydrolase L1 (UCH-L1), also known as PGP9.5, is a protein of 223 amino acids. Although it was originally characterized as a deubiquitinating enzyme, recent studies indicate that it also functions as a ubiquitin (Ub) ligase and a mono-Ub stabilizer. It is highly abundant in brain, constituting up to 2% of total brain proteins. Down-regulation and extensive oxidative modification of UCH-L1 have been observed in the brains of Alzheimer's disease (AD) and Parkinson's disease (PD) patients. Mutations in the UCH-L1 gene have been reported to be linked to Parkinson's disease, in particular, the I93 M variant is associated with a higher susceptibility of PD in contrast to a higher protection against PD for the S18Y variant. Hence, the structure of UCH-L1 and the underlying effects of disease associated mutations on the structure and function of UCH-L1 are of considerable interest. Here, we report the NMR spectral assignments of the S18Y human UCH-L1 mutant with the aim to obtain better understanding about the risk of Parkinson's disease against structural and dynamical changes induced by this mutation on UCH-L1. © 2011 The Author(s).en_HK
dc.languageengen_US
dc.publisherSpringer Netherlands. The Journal's web site is located at http://www.springer.com/physics/biophysics/journal/12104en_HK
dc.relation.ispartofBiomolecular NMR Assignmentsen_HK
dc.rightsThe Author(s)en_US
dc.rightsCreative Commons: Attribution 3.0 Hong Kong Licenseen_US
dc.subjectNMR spectroscopyen_HK
dc.subjectParkinson's diseaseen_HK
dc.subjectResonance assignmenten_HK
dc.subjectUbiquitinen_HK
dc.subjectUbiquitin carboxy-terminal hydrolase L1en_HK
dc.titleBackbone and side-chain 1H, 15N and 13C resonance assignments of S18Y mutant of ubiquitin carboxy-terminal hydrolase L1en_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4551/resserv?sid=springerlink&genre=article&atitle=Backbone and side-chain <sup>1</sup>H, <sup>15</sup>N and <sup>13</sup>C resonance assignments of S18Y mutant of ubiquitin carboxy-terminal hydrolase L1&title=Biomolecular NMR Assignments&issn=18742718&date=2011-10-01&volume=5&issue=2& spage=165&authors=Ho-Sum Tse, Hong-Yu Hu, Kong-Hung Szeen_US
dc.identifier.emailSze, KH:khsze@hku.hken_HK
dc.identifier.authoritySze, KH=rp00785en_HK
dc.description.naturepublished_or_final_versionen_US
dc.identifier.doi10.1007/s12104-011-9292-7en_HK
dc.identifier.pmid21298373-
dc.identifier.pmcidPMC3166605-
dc.identifier.scopuseid_2-s2.0-84855371939en_HK
dc.relation.referencesDas C, Hoang QQ, Kreinbring CA, Luchansky SJ, Meray RK, Ray SS, Lansbury PT, Ringe D, Petsko GA (2006) Structural basis for conformational plasticity of the Parkinson’s disease-associated ubiquitin hydrolase UCH-L1. Proc Natl Acad Sci USA 103:4675–4680en_US
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dc.relation.referencesNaito S, Mochizuki H, Yasuda T et al (2006) Characterization of multimetric variants of ubiquitin carboxyl-terminal hydrolase L1 in water by small-angle neutron scattering. Biochem Biophys Res Commun 339:717–725en_US
dc.relation.referencesdoi: 10.1016/j.bbrc.2005.11.066en_US
dc.relation.referencesOsaka H, Wang YL, Takada K et al (2003) Ubiquitin carboxy-terminal hydrolase L1 binds to and stabilizes monoubiquitin in neuron. Hum Mol Genet 12:1945–1958en_US
dc.relation.referencesdoi: 10.1093/hmg/ddg211en_US
dc.relation.referencesWilkinson KD, Lee KM, Deshpande S, Duerksen-Hughes P, Boss JM, Pohl J (1989) The neuron-specific protein PGP 9.5 is a ubiquitin carboxyl-terminal hydrolase. Science 246:670–673en_US
dc.relation.referencesWishart DS, Sykes BD (1994) The13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR 4:171–180en_US
dc.relation.referencesdoi: 10.1007/BF00175245en_US
dc.relation.referencesGoddard TD, Kneller DG (1993) SPARKY 3. University of California, San Franciscoen_US
dc.relation.referencesHibi K, Liu Q, Beaudry GA et al (1998) Serial analysis of gene expression in non-small cell lung cancer. Cancer Res 58:5690–5694en_US
dc.relation.referencesLiu Y, Fallon L, Lashuel HA, Liu Z, Lansbury PT Jr (2002) The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson’s disease susceptibility. Cell 111:209–18en_US
dc.relation.referencesMaraganore DM, Farrer MJ, Hardy JA, McDonnell SK, Lincoln SJ, Rocca WA (1999) Case-control study of the ubiquitin carboxy-terminal hydrolase L1 gene in Parkinson’s disease. Neurology 53:1858–1860en_US
dc.identifier.volume5en_US
dc.identifier.issue2en_US
dc.identifier.spage165en_HK
dc.identifier.epage168en_HK
dc.identifier.eissn1874-270Xen_US
dc.identifier.isiWOS:000294559700010-
dc.publisher.placeNetherlandsen_HK
dc.description.otherSpringer Open Choice, 21 Feb 2012en_US
dc.identifier.scopusauthoridTse, HS=36919182700en_HK
dc.identifier.scopusauthoridHu, HY=24344153500en_HK
dc.identifier.scopusauthoridSze, KH=7006735061en_HK
dc.identifier.citeulike8788812-

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