Endre søk
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf
Characterisation of Schizosaccharomyces pombe alpha-actinin
Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten).
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
2016 (engelsk)Inngår i: PeerJ, ISSN 2167-8359, E-ISSN 2167-8359, Vol. 4, artikkel-id e1858Artikkel i tidsskrift (Fagfellevurdert) Published
Resurstyp
Text
Abstract [en]

The actin cytoskeleton plays a fundamental role in eukaryotic cells. Its reorganization is regulated by a plethora of actin-modulating proteins, such as a-actinin. In higher organisms, alpha-actinin is characterized by the presence of three distinct structural domains: an N-terminal actin-binding domain and a C-terminal region with EF-hand motif separated by a central rod domain with four spectrin repeats. Sequence analysis has revealed that the central rod domain of alpha-actinin from the fission yeast Schizosaccharomyces pombe consists of only two spectrin repeats. To obtain a firmer understanding of the structure and function of this unconventional alpha-actinin, we have cloned and characterized each structural domain. Our results show that this alpha-actinin isoform is capable of forming dimers and that the rod domain is required for this. However, its actin-binding and cross-linking activity appears less efficient compared to conventional alpha-actinins. The solved crystal structure of the actin-binding domain indicates that the closed state is stabilised by hydrogen bonds and a salt bridge not present in other a-actinins, which may reduce the affinity for actin.

sted, utgiver, år, opplag, sider
2016. Vol. 4, artikkel-id e1858
Emneord [en]
Spectrin repeat, Actin-binding protein, alpha-actinin, Schizosaccharomyces pombe
HSV kategori
Identifikatorer
URN: urn:nbn:se:umu:diva-120364DOI: 10.7717/peerj.1858ISI: 000374159200008PubMedID: 27069798OAI: oai:DiVA.org:umu-120364DiVA, id: diva2:929136
Forskningsfinansiär
Carl Tryggers foundation Tilgjengelig fra: 2016-05-17 Laget: 2016-05-16 Sist oppdatert: 2018-06-07bibliografisk kontrollert

Open Access i DiVA

fulltext(108358 kB)207 nedlastinger
Filinformasjon
Fil FULLTEXT01.pdfFilstørrelse 108358 kBChecksum SHA-512
e0e9b73353a72f28faeef38bc1ab0f860073ddac56a7fa8c5600c16497f011423a6439371aef084fa8d9a5e6ddd0f78bfa00c52e41c09b6c7a3009afc2686fd5
Type fulltextMimetype application/pdf

Andre lenker

Forlagets fulltekstPubMed

Søk i DiVA

Av forfatter/redaktør
Sandblad, LindaPersson, KarinaBackman, Lars
Av organisasjonen
I samme tidsskrift
PeerJ

Søk utenfor DiVA

GoogleGoogle Scholar
Totalt: 207 nedlastinger
Antall nedlastinger er summen av alle nedlastinger av alle fulltekster. Det kan for eksempel være tidligere versjoner som er ikke lenger tilgjengelige

doi
pubmed
urn-nbn

Altmetric

doi
pubmed
urn-nbn
Totalt: 1523 treff
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf