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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

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IMPACT FACTOR 2016: 3.273

CiteScore 2016: 3.01

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1437-4315
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Volume 390, Issue 8

Issues

Protein targeting by the signal recognition particle

Przemyslaw Grudnik
  • Heidelberg University Biochemistry Center (BZH), Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Gert Bange
  • Heidelberg University Biochemistry Center (BZH), Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Irmgard Sinning
  • Heidelberg University Biochemistry Center (BZH), Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2009-06-27 | DOI: https://doi.org/10.1515/BC.2009.102

Abstract

Protein targeting by the signal recognition particle (SRP) is universally conserved and starts with the recognition of a signal sequence in the context of a translating ribosome. SRP54 and FtsY, two multidomain proteins with guanosine triphosphatase (GTPase) activity, are the central elements of the SRP system. They have to coordinate the presence of a signal sequence with the presence of a vacant translocation channel in the membrane. For coordination the two GTPases form a unique, nearly symmetric heterodimeric complex in which the activation of GTP hydrolysis plays a key role for membrane insertion of substrate proteins. Recent results are integrated in an updated perception of the order of events in SRP-mediated protein targeting.

Keywords: chloroplast SRP; guanosine triphosphatase (GTPase); membrane protein insertion; protein targeting; signal recognition particle (SRP); signal sequence; SRP; SRP receptor

About the article

Corresponding author


Received: 2009-04-07

Accepted: 2009-05-12

Published Online: 2009-06-27

Published in Print: 2009-08-01


Citation Information: Biological Chemistry, Volume 390, Issue 8, Pages 775–782, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2009.102.

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