TFIIF, a basal eukaryotic transcription factor, is a substrate for poly(ADP-ribosyl)ation - PubMed (original) (raw)
TFIIF, a basal eukaryotic transcription factor, is a substrate for poly(ADP-ribosyl)ation
J M Rawling et al. Biochem J. 1997.
Abstract
We have examined the susceptibility of some of the basal eukaryotic transcription factors as covalent targets for poly(ADP-ribosyl)ation. Human recombinant TATA-binding protein, transcription factor (TF)IIB and TFIIF (made up of the 30 and 74 kDa RNA polymerase II-associated proteins RAP30 and RAP74) were incubated with calf thymus poly(ADP-ribose) polymerase and [32P]NAD+ at 37 degrees C. On lithium dodecyl sulphate/PAGE and autoradiography, two bands of radioactivity, coincident with RAP30 and RAP74, were observed. No radioactivity co-migrated with TATA-binding protein or TFIIB. The phenomenon was dependent on the presence of nicked DNA, which is essential for poly(ADP-ribose) polymerase activity. Covalent modification of TFIIF increased with time of incubation, with increasing TFIIF concentration and with increasing NAD+ concentration. High-resolution PAGE confirmed that the radioactive species associated with RAP30 and RAP74 were ADP-ribose polymers. From these observations, we conclude that both TFIIF subunits are highly specific substrates for covalent poly(ADP-ribosyl)ation.
References
- J Biol Chem. 1981 May 10;256(9):4135-7 - PubMed
- J Biol Chem. 1993 Sep 25;268(27):20482-9 - PubMed
- Nature. 1982 Nov 25;300(5890):366-8 - PubMed
- Nature. 1982 Nov 25;300(5890):368-70 - PubMed
- J Biol Chem. 1983 May 10;258(9):5955-9 - PubMed
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Miscellaneous