Male Sterile2 Encodes a Plastid-Localized Fatty Acyl Carrier Protein Reductase Required for Pollen Exine Development in Arabidopsis

• DOI: 10.1104/pp.111.181693
• Publication Date: 2011-08-04T05:32:04Z
• Authors: Weiwei Chen; Xiao-Hong Yu; Kaisi Zhang; Jianxin Shi; Sheron De Oliveira; Lukas Schreiber; John Shanklin; Dabing Zhang
• Keywords: Transit Peptide; Acyl carrier protein

Abstract Male Sterile2 (MS2) is predicted to encode a fatty acid reductase required for pollen wall development in Arabidopsis (Arabidopsis thaliana). Transient expression of MS2 tobacco (Nicotiana benthamiana) leaves resulted the accumulation significant levels C16 and C18 alcohols. Expression fused with green fluorescent protein revealed that an amino-terminal transit peptide targets plastids. The plastidial localization biologically important because genetic complementation ms2 homozygous plants was dependent on presence its or Rubisco small subunit peptide. In addition, two domains, NAD(P)H-binding domain sterile domain, conserved homologs were also shown be essential function exine by testing. Direct biochemical analysis purified recombinant enzyme able convert palmitoyl-Acyl Carrier Protein corresponding C16:0 alcohol NAD(P)H as preferred electron donor. Using optimized reaction conditions (i.e. at pH 6.0 30°C), exhibits K m 16:0-Acyl 23.3 ± 4.0 μm, V max 38.3 4.5 nmol mg−1 min−1, catalytic efficiency/K 1,873 −1 s−1. Based high homology other characterized reductases, it surprising showed no activity against palmitoyl- acyl-coenzyme A; however, this consistent localization. summary, evidence demonstrate MS2-mediated pathway production alcohols are biosynthesis Arabidopsis.