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Title: Tandem duplications of a degenerated GTP-binding domain at the origin of GTPase receptors Toc159 and thylakoidal SRP

Abstract

The evolutionary origin of some nuclear encoded proteins that translocate proteins across the chloroplast envelope remains unknown. Therefore, sequences of GTPase proteins constituting the Arabidopsis thaliana translocon at the outer membrane of chloroplast (atToc) complexes were analyzed by means of HCA. In particular, atToc159 and related proteins (atToc132, atToc120, and atToc90) do not have proven homologues of prokaryotic or eukaryotic ancestry. We established that the three domains commonly referred to as A, G, and M originate from the GTPase G domain, tandemly repeated, and probably evolving toward an unstructured conformation in the case of the A domain. It resulted from this study a putative common ancestor for these proteins and a new domain definition, in particular the splitting of A into three domains (A1, A2, and A3), has been proposed. The family of Toc159, previously containing A. thaliana and Pisum sativum, has been extended to Medicago truncatula and Populus trichocarpa and it has been revised for Oryza sativa. They have also been compared to GTPase subunits involved in the cpSRP system. A distant homology has been revealed among Toc and cpSRP GTP-hydrolyzing proteins of A. thaliana, and repetitions of a GTPase domain were also found in cpSRP protein receptors, bymore » means of HCA analysis.« less

Authors:
 [1];  [2]
  1. Laboratorio de Biologia Molecular, CINBIN, Universidad Industrial de Santander, Bucaramanga, Apartado Aereo 678 (Colombia)
  2. Protein Structure Prediction, IMPMC, UMR 7590, Universites Paris 6 and Paris 7, Paris (France)
Publication Date:
OSTI Identifier:
21033008
Resource Type:
Journal Article
Journal Name:
Biochemical and Biophysical Research Communications
Additional Journal Information:
Journal Volume: 364; Journal Issue: 2; Other Information: DOI: 10.1016/j.bbrc.2007.10.006; PII: S0006-291X(07)02146-8; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; AMINO ACIDS; ARABIDOPSIS; CELL MEMBRANES; CHLOROPLASTS; PISUM; RECEPTORS; RICE

Citation Formats

Hernandez Torres, Jorge, Maldonado, Monica Alexandra Arias, and Chomilier, Jacques. Tandem duplications of a degenerated GTP-binding domain at the origin of GTPase receptors Toc159 and thylakoidal SRP. United States: N. p., 2007. Web. doi:10.1016/j.bbrc.2007.10.006.
Hernandez Torres, Jorge, Maldonado, Monica Alexandra Arias, & Chomilier, Jacques. Tandem duplications of a degenerated GTP-binding domain at the origin of GTPase receptors Toc159 and thylakoidal SRP. United States. https://doi.org/10.1016/j.bbrc.2007.10.006
Hernandez Torres, Jorge, Maldonado, Monica Alexandra Arias, and Chomilier, Jacques. 2007. "Tandem duplications of a degenerated GTP-binding domain at the origin of GTPase receptors Toc159 and thylakoidal SRP". United States. https://doi.org/10.1016/j.bbrc.2007.10.006.
@article{osti_21033008,
title = {Tandem duplications of a degenerated GTP-binding domain at the origin of GTPase receptors Toc159 and thylakoidal SRP},
author = {Hernandez Torres, Jorge and Maldonado, Monica Alexandra Arias and Chomilier, Jacques},
abstractNote = {The evolutionary origin of some nuclear encoded proteins that translocate proteins across the chloroplast envelope remains unknown. Therefore, sequences of GTPase proteins constituting the Arabidopsis thaliana translocon at the outer membrane of chloroplast (atToc) complexes were analyzed by means of HCA. In particular, atToc159 and related proteins (atToc132, atToc120, and atToc90) do not have proven homologues of prokaryotic or eukaryotic ancestry. We established that the three domains commonly referred to as A, G, and M originate from the GTPase G domain, tandemly repeated, and probably evolving toward an unstructured conformation in the case of the A domain. It resulted from this study a putative common ancestor for these proteins and a new domain definition, in particular the splitting of A into three domains (A1, A2, and A3), has been proposed. The family of Toc159, previously containing A. thaliana and Pisum sativum, has been extended to Medicago truncatula and Populus trichocarpa and it has been revised for Oryza sativa. They have also been compared to GTPase subunits involved in the cpSRP system. A distant homology has been revealed among Toc and cpSRP GTP-hydrolyzing proteins of A. thaliana, and repetitions of a GTPase domain were also found in cpSRP protein receptors, by means of HCA analysis.},
doi = {10.1016/j.bbrc.2007.10.006},
url = {https://www.osti.gov/biblio/21033008}, journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 2,
volume = 364,
place = {United States},
year = {Fri Dec 14 00:00:00 EST 2007},
month = {Fri Dec 14 00:00:00 EST 2007}
}