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Title: Evolution of plant δ1-pyrroline-5-carboxylate reductases from phylogenetic and structural perspectives

Proline plays a crucial role in cell growth and stress responses, and its accumulation is essential for the tolerance of adverse environmental conditions in plants. Two routes are used to biosynthesize proline in plants. The main route uses glutamate as a precursor, while in the other route proline is derived from ornithine. The terminal step of both pathways, the conversion of δ1-pyrroline-5-carboxylate (P5C) to L-proline, is catalyzed by P5C reductase (P5CR) using NADH or NADPH as a cofactor. Since P5CRs are important housekeeping enzymes, they are conserved across all domains of life and appear to be relatively unaffected throughout evolution. However, global analysis of these enzymes unveiled significant functional diversity in the preference for cofactors (NADPH vs. NADH), variation in metal dependence and the differences in the oligomeric state. In our study we investigated evolutionary patterns through phylogenetic and structural analysis of P5CR representatives from all kingdoms of life, with emphasis on the plant species. We attempted to correlate local sequence/structure variation among the functionally and structurally characterized members of the family.
Authors:
 [1] ;  [2] ;  [3] ;  [1] ;  [3]
  1. Univ. of Ferrara, Ferrara (Italy)
  2. National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD (United States)
  3. Argonne National Lab. (ANL), Argonne, IL (United States)
Publication Date:
OSTI Identifier:
1224096
Grant/Contract Number:
AC02-06CH11357
Type:
Accepted Manuscript
Journal Name:
Frontiers in Plant Science
Additional Journal Information:
Journal Volume: 6; Journal ID: ISSN 1664-462X
Publisher:
Frontiers Research Foundation
Research Org:
Argonne National Laboratory (ANL), Argonne, IL (United States)
Sponsoring Org:
USDOE
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES P5C reductase; phylogenetic analysis; 3-D structures of P5CRs; oligomer structure prediction; cofactor preference