β-Substituting alanine synthases: roles in cysteine metabolism and abiotic and biotic stress signalling in plants
Jibran Tahir A and Paul Dijkwel A B
+ Author Affiliations
- Author Affiliations
A Institute of Fundamental Sciences, Massey University, Private Bag 11222, Palmerston North, New Zealand.
B Corresponding author. Email: p.dijkwel@massey.ac.nz
Functional Plant Biology 43(4) 307-323 https://doi.org/10.1071/FP15272
Submitted: 4 September 2015 Accepted: 10 December 2015 Published: 16 February 2016
Abstract
Cysteine is required for the synthesis of proteins and metabolites, and is therefore an indispensable compound for growth and development. The β-substituting alanine synthase (BSAS) gene family encodes enzymes known as O-acetylserine thiol lyases (OASTLs), which carry out cysteine biosynthesis in plants. The functions of the BSAS isoforms have been reported to be crucial in assimilation of S and cysteine biosynthesis, and homeostasis in plants. In this review we explore the functional variation in this classic pyridoxal-phosphate-dependent enzyme family of BSAS isoforms. We discuss how specialisation and divergence in BSAS catalytic activities makes a more dynamic set of biological routers that integrate cysteine metabolism and abiotic and biotic stress signalling in Arabidopsis thaliana (L.) Heynh. and also other species. Our review presents a universal scenario in which enzymes modulating cysteine metabolism promote survival and fitness of the species by counteracting internal and external stress factors.
Additional keywords: Arabidopsis thaliana, cyanide detoxification, isoforms, O-acetyl thiol lyase, sulfur assimilation.
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