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Buchner, Johannes

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

SCImago Journal Rank (SJR) 2015: 1.607
Source Normalized Impact per Paper (SNIP) 2015: 0.751
Impact per Publication (IPP) 2015: 2.609

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PAF67, a Novel Protein That Is Associated with the Initiation-Competent Form of RNA Polymerase I

Peter Seither / Sebastian Iben / Marc Thiry / Ingrid Grummt

Citation Information: Biological Chemistry. Volume 382, Issue 8, Pages 1163–1170, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2001.146, June 2005

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Mammalian RNA polymerase I (Pol I) is a multisubunit enzyme that is decorated with accessory proteins, termed PAFs (polymeraseassociated factors). The presence or absence of distinct PAFs may account for the functional differences of distinct fractions of cellular Pol I, and suggests that PAFs could be targets of regulatory pathways. Here we describe and functionally characterize PAF67, a novel 67 kDa protein that is tightly associated with a subpopulation of cellular Pol I. Both PAF67-containing and deficient Pol I transcribe nonspecific templates with similar efficiency, however, only the enzyme that contains PAF67 is capable of specifically transcribing rDNA templates. PAF67 colocalizes with Pol I in the nucleolus at sites of active rDNA transcription, indicating that PAF67 serves a role in rDNA transcription initiation. The results suggest that association of PAF67 with the core enzyme endows Pol I with the capability to assemble into a productive transcription initiation complex at the rDNA promoter.

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