II. Yeast sequencing reports. The sequence of a 22·4 kb DNA fragment from the left arm of yeast chromosome II reveals homologues to bacterial proline synthetase and murine α-adaptin, as well as a new permease and a DNA-binding protein

REB1 is a DNA-binding protein that recognizes sites within both the enhancer and the promoter of rRNA transcription as well as upstream of many genes transcribed by RNA polymerase II. We report here the cloning of the gene for REB1 by screening a yeast genomic lambda gt11 library with specific oligonucleotides containing the REB1 binding site consensus sequence. The REB1 gene was sequenced, revealing an open reading frame encoding 809 amino acids. The predicted protein was highly hydrophilic, with numerous OH-containing amino acids and glutamines, features common to many of the general DNA-binding proteins of Saccharomyces cerevisiae, such as ABF1, RAP1, GCN4, and HSF1. There was some homology between a portion of REB1 and the DNA-binding domain of the oncogene myb. REB1 is an essential gene that maps on chromosome II. However, the physiological role that it plays in the cell has yet to be established.

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REB1, a yeast DNA-binding protein with many targets, is essential for growth and bears some resemblance to the oncogene myb

Molecular and Cellular Biology ◽

10.1128/mcb.10.10.5226-5234.1990 ◽

1990 ◽

Vol 10 (10) ◽

pp. 5226-5234

Author(s):

Q D Ju ◽

B E Morrow ◽

J R Warner

Keyword(s):

Amino Acids ◽

Dna Binding ◽

Rna Polymerase Ii ◽

Essential Gene ◽

Binding Protein ◽

Consensus Sequence ◽

Physiological Role ◽

Dna Binding Protein ◽

Reading Frame ◽

Chromosome Ii

REB1 is a DNA-binding protein that recognizes sites within both the enhancer and the promoter of rRNA transcription as well as upstream of many genes transcribed by RNA polymerase II. We report here the cloning of the gene for REB1 by screening a yeast genomic lambda gt11 library with specific oligonucleotides containing the REB1 binding site consensus sequence. The REB1 gene was sequenced, revealing an open reading frame encoding 809 amino acids. The predicted protein was highly hydrophilic, with numerous OH-containing amino acids and glutamines, features common to many of the general DNA-binding proteins of Saccharomyces cerevisiae, such as ABF1, RAP1, GCN4, and HSF1. There was some homology between a portion of REB1 and the DNA-binding domain of the oncogene myb. REB1 is an essential gene that maps on chromosome II. However, the physiological role that it plays in the cell has yet to be established.

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A Centromere DNA-binding Protein from Fission Yeast Affects Chromosome Segregation and Has Homology to Human CENP-B

The Journal of Cell Biology ◽

10.1083/jcb.136.3.487 ◽

1997 ◽

Vol 136 (3) ◽

pp. 487-500 ◽

Cited By ~ 35

Author(s):

Dana Halverson ◽

Mary Baum ◽

Janet Stryker ◽

John Carbon ◽

Louise Clarke

Keyword(s):

Dna Binding ◽

Fission Yeast ◽

Mitotic Chromosome ◽

Binding Protein ◽

Chromosome Instability ◽

Dna Binding Protein ◽

Autonomously Replicating Sequence ◽

Human Centromere ◽

Chromosome Ii

Genetic and biochemical strategies have been used to identify Schizosaccharomyces pombe proteins with roles in centromere function. One protein, identified by both approaches, shows significant homology to the human centromere DNA-binding protein, CENP-B, and is identical to Abp1p (autonomously replicating sequence-binding protein 1) (Murakami, Y., J.A. Huberman, and J. Hurwitz. 1996. Proc. Natl. Acad. Sci. USA. 93:502–507). Abp1p binds in vitro specifically to at least three sites in centromeric central core DNA of S. pombe chromosome II (cc2). Overexpression of abp1 affects mitotic chromosome stability in S. pombe. Although inactivation of the abp1 gene is not lethal, the abp1 null strain displays marked mitotic chromosome instability and a pronounced meiotic defect. The identification of a CENP-B–related centromere DNA-binding protein in S. pombe strongly supports the hypothesis that fission yeast centromeres are structurally and functionally related to the centromeres of higher eukaryotes.

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