Two nucleosome binding proteins with similar nucleosome-binding properties and similar modulating activities on promoter chromatin architecture proofed to play distinct roles in the determination of target gene transcription and thus the final gene expression in vivo.

The proteins analysed by scientists from the Cornell University (USA) were histone H1 and poly(ADP-ribose) polymerase-1 (PARP-1). They discovered that the two molecules show a reciprocal pattern of chromatin binding at many RNA polymerase II-transcribed promoters: PARP-1 was more frequent associated with the promoter when histone H1 binding was diminished at the same time. The pattern could be linked to presently transcribed genes. Also, PARP-1 seems to exclude H1 actively from some of the PARP-1 stimulated promoters. This points at a functional interplay between PARP-1 and H1 in regard to nucleosome binding.

Related antibodies on antibodies-online.com:

PARP-1

Histone H1

RNA Polymerase II

PARP

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