BRMS151-98 and BRMS151-84 are crystal oligomeric coiled coils with different oligomerization states, which behave as disordered protein fragments in solution

17 páginas, 9 figuras, 1 tabla.

Detalles Bibliográficos
Autores: Spínola-Amilibia, Mercedes, Rivera, José, Ortiz-Lombardía, Miguel, Romero, Antonio, Neira, José L., Bravo, Jerónimo
Tipo de recurso: artículo
Fecha de publicación:2013
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/83505
Acceso en línea:http://hdl.handle.net/10261/83505
Access Level:acceso abierto
Palabra clave:X-ray
Coiled coils
NMR
BRMS1
biophysical features
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spelling BRMS151-98 and BRMS151-84 are crystal oligomeric coiled coils with different oligomerization states, which behave as disordered protein fragments in solutionSpínola-Amilibia, MercedesRivera, JoséOrtiz-Lombardía, MiguelRomero, AntonioNeira, José L.Bravo, JerónimoX-rayCoiled coilsNMRBRMS1biophysical features17 páginas, 9 figuras, 1 tabla.The breast cancer metastasis suppressor 1 (BRMS1) gene suppresses metastasis without affecting the primary tumor growth. Cellular localization of BRMS1 appears to be important for exerting its effects on metastasis inhibition. We recently described a nucleo-cytoplasmic shuttling for BRMS1 and identified a nuclear export signal within the N-terminal coiled coil. The structure of these regions shows an antiparallel coiled coil capable of oligomerizing, which compromises the accessibility to the nuclear export signal consensus residues. We have studied the structural and biophysical features of this region to further understand the contribution of the N-terminal coiled coil to the biological function of BRMS1. We have observed that residues 85 to 98 might be important in defining the oligomerization state of the BRMS1 N-terminal coiled coil. The fragments are mainly disordered in solution, with evidence of residual structure. In addition, we report the presence of a conformational dynamic equilibrium (oligomeric folded species ↔ oligomeric unfolded) in solution in the BRMS1 N-terminal coiled coil that might facilitate the nuclear export of BRMS1 to the cytoplasm.Work at the J.L.N. laboratory was supported by the Spanish Ministerio de Ciencia e Innovación (CTQ2011-24393, CSD2008-00005) and intramural BIFI 2011 grant. Work at the J.B. laboratory was supported by Ministerio de Ciencia e Innovación (SAF2008-04048-E, SAF2009-10667, and SAF2012-31405), Conselleria de Sanitat, Generalitat Valenciana AP-001/10, CSIC (200820I020), and Fundación Mutua Madrileña, Spain.Peer reviewedElsevier201320132013info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501http://hdl.handle.net/10261/83505reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1016/j.jmb.2013.03.005info:eu-repo/semantics/openAccessoai:digital.csic.es:10261/835052026-05-22T06:33:51Z
dc.title.none.fl_str_mv BRMS151-98 and BRMS151-84 are crystal oligomeric coiled coils with different oligomerization states, which behave as disordered protein fragments in solution
title BRMS151-98 and BRMS151-84 are crystal oligomeric coiled coils with different oligomerization states, which behave as disordered protein fragments in solution
spellingShingle BRMS151-98 and BRMS151-84 are crystal oligomeric coiled coils with different oligomerization states, which behave as disordered protein fragments in solution
Spínola-Amilibia, Mercedes
X-ray
Coiled coils
NMR
BRMS1
biophysical features
title_short BRMS151-98 and BRMS151-84 are crystal oligomeric coiled coils with different oligomerization states, which behave as disordered protein fragments in solution
title_full BRMS151-98 and BRMS151-84 are crystal oligomeric coiled coils with different oligomerization states, which behave as disordered protein fragments in solution
title_fullStr BRMS151-98 and BRMS151-84 are crystal oligomeric coiled coils with different oligomerization states, which behave as disordered protein fragments in solution
title_full_unstemmed BRMS151-98 and BRMS151-84 are crystal oligomeric coiled coils with different oligomerization states, which behave as disordered protein fragments in solution
title_sort BRMS151-98 and BRMS151-84 are crystal oligomeric coiled coils with different oligomerization states, which behave as disordered protein fragments in solution
dc.creator.none.fl_str_mv Spínola-Amilibia, Mercedes
Rivera, José
Ortiz-Lombardía, Miguel
Romero, Antonio
Neira, José L.
Bravo, Jerónimo
author Spínola-Amilibia, Mercedes
author_facet Spínola-Amilibia, Mercedes
Rivera, José
Ortiz-Lombardía, Miguel
Romero, Antonio
Neira, José L.
Bravo, Jerónimo
author_role author
author2 Rivera, José
Ortiz-Lombardía, Miguel
Romero, Antonio
Neira, José L.
Bravo, Jerónimo
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv X-ray
Coiled coils
NMR
BRMS1
biophysical features
topic X-ray
Coiled coils
NMR
BRMS1
biophysical features
description 17 páginas, 9 figuras, 1 tabla.
publishDate 2013
dc.date.none.fl_str_mv 2013
2013
2013
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/83505
url http://hdl.handle.net/10261/83505
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1016/j.jmb.2013.03.005
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869424001627979776
score 15.812429

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