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A new ‘paralyzed’ flagella mutant, OC‐10, in Chlamydomonas reinhardtii (Volvocales, Chlorophyceae) that can be reactivated with adenosine triphosphate
Author(s) -
Nakamura Shogo,
Kawanishi Emiko,
Nakamura Soichi,
Watanabe Shin,
Kojima Manabu K.
Publication year - 1995
Publication title -
phycological research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.438
H-Index - 44
eISSN - 1440-1835
pISSN - 1322-0829
DOI - 10.1111/j.1440-1835.1995.tb00006.x
Subject(s) - flagellum , chlamydomonas reinhardtii , biology , chlamydomonas , motility , mutant , microbiology and biotechnology , adenosine triphosphate , biochemistry , gene
SUMMARY A new ‘paralyzed’ mutant. OC–10, was isolated in Chlamydomonas reinhardtii Dangeard. OC‐10 cannot swim and generally shows very little flagellar movement. However, when OC‐10 was demembranated, axonemal motility was reactivated in the presence of adenosine triphosphate (ATP) or adenosine diphosphate (ADP). The beating form of the reactivated axonemes was almost the same as that of the wild‐type axonemes. Flagellar regeneration of OC‐10 was slower than that of the wild‐type. Electron microscopic examination showed no abnormality in OC‐10 flagella, but SDS/PAGE revealed that mobility of a flagellar membrane protein was changed and a few bands disappeared in OC‐10 flagella, When the mutant was crossed to wild‐type to form temporary dikaryon cells with 4 flagella, OC‐10 flagella did not regain motility. Tetrad analysis of crosses between OC–10 and wild‐type demonstrated a 1:1 segregation on the basis of flagellar motility. From these results, we suppose that OC‐10 may be limited in ATP availability inside the flagella, or altered in flagellar membrane proteins important for motility.