DNA-binding domain of RCC1 protein is not essential for coupling mitosis with DNA replication

H. Seino, N. Hisamoto, S. Uzawa, T. Sekiguchi, T. Nishimoto

Research output: Contribution to journalArticle

48 Citations (Scopus)

Abstract

The RCC1 protein that is required for coupling mitosis with the S phase has a DNA-binding domain in the N-terminal region outside the repeat. We found that RCC1 protein without any DNA-binding activity complemented the tsBN2 mutation with the same efficiency as that of intact RCC1 protein. In ts+ transformants of tsBN2 cells transfected with the RCC1 cDNA lacking the DNA-binding domain, an endogenous RCC1 disappeared at 39.5°C, and the deleted RCC1 protein encoded by the transfected cDNA was found in the cytoplasm, but a significant amount of it was also found in the nuclei. This deleted RCC1 protein was eluted from the nuclei with the same concentration of NaCl and DNase I as was used for the intact RCC1 protein in BHK21 cells. Furthermore, the deleted RCC1 protein co-migrated with the nucleosome fraction on sucrose density gradient analysis. These results indicate that the RCC1 protein binds chromatin with the aid of other unknown protein(s). Thus, the DNA-binding domain of RCC1 protein is not essential for coupling between the S and M phases, but was shown instead to function as a nuclear translocation signal.

Original languageEnglish
Pages (from-to)393-400
Number of pages8
JournalJournal of cell science
Volume102
Issue number3
Publication statusPublished - 1992
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Cell Biology

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