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

Forlani, Giuseppe; Makarova, Kira S.; Ruszkowski, Milosz; Bertazzini, Michele; Nocek, Boguslaw

doi:10.3389/fpls.2015.00567

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

Journal Article · Mon Aug 03 00:00:00 EDT 2015 · Frontiers in Plant Science

DOI:https://doi.org/10.3389/fpls.2015.00567· OSTI ID:1224096

Forlani, Giuseppe ^[1]; Makarova, Kira S. ^[2]; Ruszkowski, Milosz ^[3]; Bertazzini, Michele ^[1]; Nocek, Boguslaw ^[3]

Univ. of Ferrara, Ferrara (Italy)
National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD (United States)
Argonne National Lab. (ANL), Argonne, IL (United States)

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.

View Accepted Manuscript (DOE)

Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: USDOE

Grant/Contract Number:: AC02-06CH11357

OSTI ID:: 1224096

Journal Information:: Frontiers in Plant Science, Journal Name: Frontiers in Plant Science Vol. 6; ISSN 1664-462X

Publisher:: Frontiers Research FoundationCopyright Statement

Country of Publication:: United States

Language:: English

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Related Subjects

3-D structures of P5CRs
59 BASIC BIOLOGICAL SCIENCES
P5C reductase
cofactor preference
oligomer structure prediction
phylogenetic analysis