Skip Navigation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Terao, T.
Right arrow Articles by Katoh, S.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Terao, T.
Right arrow Articles by Katoh, S.
Agricola
Right arrow Articles by Terao, T.
Right arrow Articles by Katoh, S.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Plant and Cell Physiology, 1985, Vol. 26, No. 7 1369-1377
© 1985


Article

Chlorophyll b-Deficient Mutants of Rice

II. Antenna Chlorophyll a/b-Proteins of Photosystem I and II

Tomio Terao1, Atsushi Yamashita2 and Sakae Katoh3

1Department of Applied Physiology, National Institute of Agrobiological Resources Tsukuba Science City, Ibaragi 305, Japan
2Department of Moleculer Biology, National Institute of Agrobiological Resources Tsukuba Science City, Ibaragi 305, Japan
3Department of Pure and Applied Sciences, College of Arts and Sciences, University of Tokyo Komaba, Meguroku, Tokyo 153, Japan

Chlorophyll-protein complexes of the wild type and 16 strains of chlorina mutants of rice were investigated by gel electrophoresis. An antenna chlorophyll a/b-protein of photosystem II (LHC-II) was present in reduced amounts in Type II chlorina mutants which have the chlorophyll a/b ratios of 10–15, and was totally absent from Type I chlorina mutants which lack chlorophyll b. Another antenna chlorophyll-protein of photosystem I (LHC-I) containing two polypeptides of 20 and 21 kDa was also present in the Type II mutants but not in the Type I mutants. The polypeptide profiles of the thylakoid membranes indicate that Type I mutants lack both the 20 and 21 kDa polypeptides, whereas the abundance of the two polypeptides relative to the CPI apoprotein in the Type II mutants is comparable with that in the wild type. It is concluded that the 20 and 21 kDa polypeptides are both related to LHC-I and are normally synthesized and accumulated in the Type II mutants.

(Received June 6, 1985; Accepted August 6, 1985)
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.