Abstract

The abnormal furrow (af) gene was identified through a maternal effect mutation that causes a defect in cell division in Xenopus embryos. In eggs obtained from mutant females (af eggs), polar body formation and cytokinesis are completely inhibited while nuclear division continues uninterrupted. Cleavage furrows are recognized as unpigmented narrow bands on the egg surface but they do not contract. Transfer of cytoplasm from wild-type eggs into af eggs partially rescues contraction of the cleavage furrow. The factor responsible for contraction promoting activity was present in wild-type eggs throughout the first cell division cycle and induced contraction in a dose dependent manner. The factor was characterized as a high molecu- lar weight protein complex that was associated with particulate fraction in the extract. The recovery of con- traction was associated with accumulation of filamentous actin and WGA-binding sites within the cleavage furrow of the af eggs which were normally not enriched for these components. Formation and contraction of a filamentous actin ring during cortical wound healing in af eggs was indistinguishable from that of wild-type eggs. From these results, the af gene product may be specifically required for reorganization of the actin filaments and WGA-binding sites in the cleavage furrow and contraction through these structures during cytokinesis.

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