Abstract
Genes encoding both the 66- and the 43-kDa subunits of yeast RNA polymerase II initiation factor a, designated TFA1 and TFA2, have been isolated. Both genes are essential for cell viability. The bacterially expressed gene products could replace factor a in transcription in vitro, and both recombinant subunits were required for activity. The deduced amino acid sequences of the TFA1 and TFA2 gene products were homologous to those of the large and small subunits of human TFIIE, respectively, identifying factor a as the yeast homolog of TFIIE.
Highlights
Genes encoding both the66-and the 43-kDa subunits quencing were required to clariftyhe relationships
The behavior of the recombinant subunits intranscription wasconsistent with that previously reported for factor a polypeptides isolated by reverse-phase HPLC [11]and confirms that TFAl and TFA2 encode the 66- and 43-kDa subunits of yeast TFIIE
Yeast factor a is identified as the homolog of vertebrate TFIIE on the basis of the similarity in amino acid sequences, as
Summary
From the Department of Cell Biology, Stanford University School of Medicine, Stanford, California 94305 Genes encoding both the66-and the 43-kDa subunits quencing were required to clariftyhe relationships. Yeast factor of yeast RNA polymerase I1 initiation factor a, desig- a consists of two highly charged polypeptides with apparent nated TFAl and TFA2, have been isolated. Both genes molecular massesof 66 and 43 kDa [11]. The deduced amino acid sequencoefsthe TFAl and TFA2 gene products were homologous to those of the large and small subunits of human TFIIE, respectively, identifying factor a as the yeast ohfomTFoIlIoEg. encode the 66- and 43-kDa subunits of factor a, respectively.
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