Purification of DNA polymerase II stimulatory factor I, a yeast single-stranded DNA-binding protein

Incidental to the purification of yeast DNA polymerase II was the observation that various chromatographic fractions contained activities that stimulated synthesis by this polymerase. In this paper we report the purification and initial characterization of one such factor, stimulatory factor I (SFI)...

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Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 1990-01, Vol.87 (2), p.677-681
Hauptverfasser: Brown, W.C. (California Institute of Technology, Pasadena, CA), Smiley, J.K, Campbell, J.L
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Sprache:eng
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Zusammenfassung:Incidental to the purification of yeast DNA polymerase II was the observation that various chromatographic fractions contained activities that stimulated synthesis by this polymerase. In this paper we report the purification and initial characterization of one such factor, stimulatory factor I (SFI). SFI, which is associated with an apparent complex of three polypeptides of 66, 37, and 13.5 kDa, binds preferentially to single-stranded DNA, possibly explaining its ability to stimulate DNA polymerase II. Single-stranded DNA-binding activity is associated with the 66-kDa polypeptide.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.87.2.677