LOSS OF A HISTIDINE RESIDUE AT THE ACTIVE-SITE OF S-LOCUS RIBONUCLEASE IS ASSOCIATED WITH SELF-COMPATIBILITY IN LYCOPERSICON-PERUVIANUM

被引:126
作者
ROYO, J
KUNZ, C
KOWYAMA, Y
ANDERSON, M
CLARKE, AE
NEWBIGIN, E
机构
[1] UNIV MELBOURNE,SCH BOT,PLANT CELL BIOL RES CTR,PARKVILLE,VIC 3052,AUSTRALIA
[2] INRA,METAB PHYSIOL & BIOCHIM VEGTALES LAB,F-78026 VERSAILLES,FRANCE
[3] MIE UNIV,FAC BIORESOURCES,TSU,MIE 514,JAPAN
关键词
D O I
10.1073/pnas.91.14.6511
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Gametophytic self-incompatibility in the Solanaceae is controlled by a single, multiallelic locus, the S locus. We have recently described an allele of the S locus of Lycopersicon peruvianum that caused this normally self-incompatible plant to become self-compatible. We have now characterized two glycoproteins present in the styles of self-compatible and self-incompatible accessions of L. peruvianum: one is a ribonuclease that cosegregates with a functional self incompatibility allele (S-6 allele); the other cosegregates with the self-compatible allele (S-c allele) but has no ribonuclease activity. The derived amino acid sequences of the cDNAs encoding the S-6 and S-c glycoproteins resemble sequences of other ribonucleases encoded by the S locus. The derived sequence for the S-c glycoprotein differs from the others by lacking one of the histidine residues found in all other S-locus ribonucleases. These findings demonstrate the essential role of ribonuclease activity in self incompatibility and lend further weight to evidence that this histidine residue is involved in the catalytic site of the enzyme.
引用
收藏
页码:6511 / 6514
页数:4
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