Identification of a 3'-->5' exonuclease activity associated with human RNA polymerase II. | Zendy

D Wang | Zendy; Diane K. Hawley | Zendy

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Identification of a 3'-->5' exonuclease activity associated with human RNA polymerase II.

Author(s) -

D Wang,

Diane K. Hawley

Publication year - 1993

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.90.3.843

Subject(s) - transcription factor ii f , rna polymerase ii , exonuclease , transcription factor ii d , polymerase , microbiology and biotechnology , rna polymerase , transcription (linguistics) , rna polymerase ii holoenzyme , rna polymerase i , biology , rna , transcription factor ii e , rna dependent rna polymerase , chemistry , biochemistry , dna , gene expression , gene , promoter , linguistics , philosophy

Human RNA polymerase II is shown to be associated with a 3'-->5' exonuclease activity that removes nucleoside 5'-monophosphates from the 3' end of the transcripts in isolated ternary complexes. This activity is stimulated by SII, a protein that acts as a transcription elongation factor in vitro. In addition, we show that another transcription factor, TFIIF, stimulates a competing pyrophosphorolysis reaction. These findings raise interesting questions about the roles of these activities in vivo, including the possibility that this RNA polymerase may proofread the nascent transcript.

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