Purification, gene cloning, and gene disruption of the transcription elongation factor S-II in Saccharomyces cerevisiae.
Saccharomyces cerevisiae S-II was purified to near homogeneity as a protein stimulating RNA polymerase II. Four of seven lysyl endopeptidase-digested fragments of S-II were located in the PPR2 sequence reported previously. Analysis of a genomic clone of S-II revealed that S-II and PPR2 are the same protein consisting of 309 amino acid residues, and frame shifts were found in the sequence of PPR2 gene reported previously. Yeast S-II and mouse S-II showed high similarity in their amino acid sequences, especially in their amino-terminal and carboxyl-terminal regions. A gene disruption experiment showed that an S-II null mutant was not lethal under usual growth conditions, indicating that S-II is not essential for the growth of yeast.
Nakanishi
T
T
Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
Nakano
A
A
Nomura
K
K
Sekimizu
K
K
Natori
S
S
D000595:Amino Acid Sequence; D001483:Base Sequence; D015139:Blotting, Southern; D003001:Cloning, Molecular; D004271:DNA, Fungal; D004268:DNA-Binding Proteins; D016368:Frameshift Mutation; D005656:Fungal Proteins / Q000235:genetics* / Q000302:isolation & purification; D005804:Genes, Lethal; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification; D015183:Restriction Mapping; D012441:Saccharomyces cerevisiae / Q000254:growth & development / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins; D012689:Sequence Homology, Nucleic Acid
D004271:DNA, Fungal; D004268:DNA-Binding Proteins; C068394:DST1 protein, S cerevisiae; D005656:Fungal Proteins; D011994:Recombinant Proteins; D029701:Saccharomyces cerevisiae Proteins