期刊
PLANT CELL
卷 22, 期 12, 页码 4067-4083出版社
OXFORD UNIV PRESS INC
DOI: 10.1105/tpc.110.080036
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资金
- Centre National de la Recherche Scientifique
- Universitede Strasbourg
- Region Alsace
- INRA
- Tepral Company
- Ministere de l'Education Nationale, de l'Enseignement Superieur et de la Recherche
- Natural Sciences and Engineering Research Council
The precise structure of the sporopollenin polymer that is the major constituent of exine, the outer pollen wall, remains poorly understood. Recently, characterization of Arabidopsis thaliana genes and corresponding enzymes involved in exine formation has demonstrated the role of fatty acid derivatives as precursors of sporopollenin building units. Fatty acyl-CoA esters synthesized by ACYL-COA SYNTHETASE5 (ACOS5) are condensed with malonyl-CoA by POLYKETIDE SYNTHASE A (PKSA) and PKSB to yield alpha-pyrone polyketides required for exine formation. Here, we show that two closely related genes encoding oxidoreductases are specifically and transiently expressed in tapetal cells during microspore development in Arabidopsis anthers. Mutants compromised in expression of the reductases displayed a range of pollen exine layer defects, depending on the mutant allele. Phylogenetic studies indicated that the two reductases belong to a large reductase/dehydrogenase gene family and cluster in two distinct clades with putative orthologs from several angiosperm lineages and the moss Physcomitrella patens. Recombinant proteins produced in bacteria reduced the carbonyl function of tetraketide alpha-pyrone compounds synthesized by PKSA/B, and the proteins were therefore named TETRAKETIDE alpha-PYRONE REDUCTASE1 (TKPR1) and TKPR2 (previously called DRL1 and CCRL6, respectively). TKPR activities, together with those of ACOS5 and PKSA/B, identify a conserved biosynthetic pathway leading to hydroxylated alpha-pyrone compounds that were previously unknown to be sporopollenin precursors.
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