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- Title
A relic S-RNase is expressed in the styles of self-compatibleNicotiana sylvestris.
- Authors
Golz, John F.; Clarke, Adrienne E.; Newbigin, Ed; Anderson, Marilyn
- Abstract
Summary:We surveyed ribonuclease activity in the styles ofNicotianaspp. and found little or no activity in self-compatible species and in a self-compatible accession of a self-incompatible species. All self-incompatible species had high levels of ribonuclease activity in their style. Interestingly, one self-compatible species,N. sylvestris, had a level of stylar ribonuclease activity comparable to that of some self-incompatibleNicotianaspecies. A ribonuclease with biochemical properties similar to those of the self-incompatibility (S-)RNases ofN. alatawas purified fromN. sylvestrisstyles. The N-terminal sequence of this protein was used to confirm the identity of a cDNA corresponding to the stylar RNase. The amino acid sequence deduced from the cDNA was related to those of the S-RNases and included the five conserved regions characteristic of these proteins. It appears that theN. sylvestrisRNase may have evolved from the S-RNases and is an example of a ‘relic S-RNase’. A number of features distinguish theN. sylvestrisRNase from the S-RNases, and the role these may have played in the presumed loss of the self-incompatibility response during the evolution of this species are discussed..
- Subjects
RIBONUCLEASES; NICOTIANA; BIOCHEMICAL mechanism of action
- Publication
Plant Journal, 1998, Vol 16, Issue 5
- ISSN
0960-7412
- Publication type
Article
- DOI
10.1046/j.1365-313x.1998.00331.x