Multiple actin-related proteins of Saccharomyces cerevisiae are present in the nucleus

Masahiko Harata, Yukako Oma, Teruko Tabuchi, Yan Zhang, David J. Stillman, Shigeki Mizuno

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53 Citations (Scopus)


An increasing number of actin-related proteins (Arps), which share the basal structure with skeletal actin but possess distinct functions, have been found in a wide variety of organisms. Individual Arps of Saccharomyces cerevisiae were classified into Arps 1-10 based on the relatedness of their sequences and functions, where Arp1 is the most similar to actin, and Arp10 is the least similar. While Arps 1-3 and their orthologs in other organisms are localized exclusively in the cytoplasm, Arp4 (also known as Act3) is localized in the nucleus and is involved in transcriptional regulation. Here we examined the more divergent Arps for possible nuclear functions. We show that Arps 5-9 are localized in the nucleus, but Arp10 is not. The nuclear export signals identified in actin are well conserved in the cytoplasmic Arps, Arps 1-3, but less conserved in the nuclear Arps. Gel filtration chromatography experiments show that the nuclear Arps are larger than monomer in size and thus are present in multi-protein complexes. Since nuclear protein complexes containing Arps are found to be responsible for histone acetylation and chromatin remodeling, it is suggested that most of the divergent Arps are involved in the transcriptional regulation through chromatin modulation.

Original languageEnglish
Pages (from-to)665-671
Number of pages7
JournalJournal of Biochemistry
Issue number4
Publication statusPublished - 2000


  • Actin-related protein
  • Chromatin
  • Nuclear localization
  • Protein complex
  • Transcriptional regulation


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