Sequence-specific binding of the Schizosaccharomyces pombe His1 protein to fission yeast telomeric DNA.
Sequence-specific protein-DNA interaction is critical for many important cellular processes such as transcription, DNA replication, and chromosome segregation. Identification of additional proteins that bind to DNA in a sequence-specific manner will contribute to the understanding of the mechanism of molecular recognition between protein and DNA. We found that the ATP phosphoribosyl transferase His1, which catalyzes the first step in histidine biosynthesis, is bound to both single- and double-stranded telomeric DNA. Competition experiments revealed that His1 is bound to a fission yeast telomeric DNA in a sequence-specific manner. Previously identified sequence-specific telomere-binding proteins contain Myb domain. In contrast, Schizosaccharomyces pombe His1 does not contain Myb domain. These findings indicate that His1 has a novel DNA-recognition domain.
Tomita
Kazunori
K
Department of Chemistry, Shizuoka University, 836 Oya, Shizuoka 422-8529, Japan.
Uritani
Masahiro
M
Ushimaru
Takashi
T
Yoshinaga
Koichi
K
Ueno
Masaru
M
D000595:Amino Acid Sequence; D004247:DNA / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D011485:Protein Binding / Q000502:physiology; D029702:Schizosaccharomyces pombe Proteins / Q000235:genetics* / Q000378:metabolism; D017422:Sequence Analysis, DNA / Q000379:methods; D016615:Telomere / Q000235:genetics / Q000378:metabolism; D034501:Telomere-Binding Proteins / Q000235:genetics* / Q000378:metabolism
D029702:Schizosaccharomyces pombe Proteins; D034501:Telomere-Binding Proteins; D004247:DNA