A rho-like protein is involved in the organisation of the contractile ring in dividing sand dollar eggs

Sand dollar eggs were microinjected with botulinum C3 exoenzyme, an ADP-ribosyltransferase from Clostridium botulinum that specifically ADP-ribosylates and inactivates rho proteins. C3 exoenzyme microinjected during nuclear division interfered with subsequent cleavage furrow formation. No actin fila...

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Bibliographic Details
Published in:Zygote (Cambridge) 1993-11, Vol.1 (4), p.325-331
Main Authors: Mabuchi, Issei, Hamaguchi, Yukihisa, Fujimoto, Hirotaka, Morii, Narito, Mishima, Masanori, Narumiya, Shuh
Format: Article
Language:English
Subjects:
Actin filaments
Actins - metabolism
ADP Ribose Transferases - pharmacology
Animals
Botulinum Toxins
C3 exoenzyme
Cell Division - drug effects
Cytokinesis
Female
Fertilization - physiology
GTP-Binding Proteins - metabolism
Ovum - drug effects
Ovum - metabolism
Poly(ADP-ribose) Polymerases - pharmacology
rho GTP-Binding Proteins
Sea Urchins - metabolism
Small G-protein
Zygote - cytology
Zygote - drug effects
Zygote - metabolism
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Summary:Sand dollar eggs were microinjected with botulinum C3 exoenzyme, an ADP-ribosyltransferase from Clostridium botulinum that specifically ADP-ribosylates and inactivates rho proteins. C3 exoenzyme microinjected during nuclear division interfered with subsequent cleavage furrow formation. No actin filaments were detected in the equatorial cortical layer of these eggs by rhodamine-phalloidin staining. When microinjected into furrowing eggs, C3 exoenzyme rapidly disrupted the contractile ring actin filaments and caused regression of the clevage furrows. C3 exoenzyme had no apparent effect on nuclear division, however, and multinucleated embryos developed from the microinjected eggs. By contrast, C3 exoenzyme did not affect the organisation of cortical actin filaments immediately after fertilisation. Only one protein (molecular weight 22000) was ADP-ribosylated by C3 exoenzyme in the isolated cleavage furrow. This protein co-migrated with ADP-ribosylated rhoA derived from human paltelets when analysed by two-dimensional gel electrophoresis. These results strongly suggest that a rho-like, small GTP-binding protein is selectively in the organisation and maintenance of the contractile ring.
ISSN:0967-1994
1469-8730
DOI:10.1017/S0967199400001659