Amino acid substitutions around the chromophore of the chromoprotein Rtms5 influence polypeptide cleavage

Turcic, Kristina, Pettikiriarachchi, Anne, Battad, Jion, Wilmann, Pascal G., Rossjohn, Jamie, Dove, Sophie G., Devenish, Rodney J. and Prescott, Mark (2006) Amino acid substitutions around the chromophore of the chromoprotein Rtms5 influence polypeptide cleavage. Biochemical And Biophysical Research Communications, 340 4: 1139-1143.


Author Turcic, Kristina
Pettikiriarachchi, Anne
Battad, Jion
Wilmann, Pascal G.
Rossjohn, Jamie
Dove, Sophie G.
Devenish, Rodney J.
Prescott, Mark
Title Amino acid substitutions around the chromophore of the chromoprotein Rtms5 influence polypeptide cleavage
Journal name Biochemical And Biophysical Research Communications  (ERA 2012 Listed)    (ERA 2010 Rank B)   Check publisher's open access policy
Publication date 2006
Sub-type Article
DOI 10.1016/j.bbrc.2005.12.118
Volume number 340
Issue number 4
ISSN 0006-291X
Start page 1139
End page 1143
Total pages 5
Editor W. Baumeister
Place of publication San Diego
Publisher Academic Press Inc Elsevier Science
Collection year 2006
Language eng
Subject C1
270199 Biochemistry and Cell Biology not elsewhere classified
780105 Biological sciences
Abstract Extension of the conjugated pi-system of many all-protein chromophores with an acylimine bond is the basis for their red-shifted optical properties. The presence of this post-translational modification is evident in crystal structures of these proteins. Harsh denaturation of proteins containing an acylimine bond results in partial polypeptide cleavage. For the red fluorescent protein DsRed, the extent of cleavage is quantitative. However, this is not the case for the blue non-fluorescent chromoprotein Rtms5, even though all chromophores in tetrameric Rtms5 contain an acylimine bond. We have identified two positions around the chromophore of Rtms5 where substitutions can promote or suppress the extent of cleavage on harsh denaturation. We propose a model in which cleavage of Rtms5 is facilitated by a trans to cis isomerisation of the chromophore. (c) 2006 Elsevier Inc. All rights reserved.
Keyword Biochemistry & Molecular Biology
Biophysics
All-protein Chromophores
Rtms5
Chromoprotein
Structure
Acylimine Bond
Red Fluorescent Protein
Gfp-like Proteins
Crystal-structure
Anemonia-sulcata
Resolution
Coral
Q-Index Code C1
Additional Notes DOI: 10.1016/j.bbrc.2005.12.118

 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 8 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 8 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Access Statistics: 92 Abstract Views  -  Detailed Statistics
Created: Wed, 15 Aug 2007, 08:24:25 EST