---
pmid: '10454562'
title: MCM proteins are associated with RNA polymerase II holoenzyme.
authors:
- Yankulov K
- Todorov I
- Romanowski P
- Licatalosi D
- Cilli K
- McCracken S
- Laskey R
- Bentley DL
journal: Mol Cell Biol
year: '1999'
full_text_available: false
pmcid: PMC84545
doi: 10.1128/MCB.19.9.6154
pubmed_publication_types:
- Journal Article
- Research Support, Non-U.S. Gov't
- Research Support, U.S. Gov't, P.H.S.
publication_type: PRIMARY_RESEARCH
---

# MCM proteins are associated with RNA polymerase II holoenzyme.
**Authors:** Yankulov K, Todorov I, Romanowski P, Licatalosi D, Cilli K, McCracken S, Laskey R, Bentley DL
**Journal:** Mol Cell Biol (1999)
**DOI:** [10.1128/MCB.19.9.6154](https://doi.org/10.1128/MCB.19.9.6154)
**PMC:** [PMC84545](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC84545/)

## Abstract

1. Mol Cell Biol. 1999 Sep;19(9):6154-63. doi: 10.1128/MCB.19.9.6154.

MCM proteins are associated with RNA polymerase II holoenzyme.

Yankulov K(1), Todorov I, Romanowski P, Licatalosi D, Cilli K, McCracken S,
Laskey R, Bentley DL.

Author information:
(1)Department of Molecular Biology and Genetics, University of Guelph, Guelph,
Ontario N1G 2W1, Canada. yankulov@uoguelph.ca

MCMs are a family of proteins related to ATP-dependent helicases that bind to
origin recognition complexes and are required for initiation of DNA replication.
We report that antibodies against MCM2(BM28) specifically inhibited
transcription by RNA polymerase II (Pol II) in microinjected Xenopus oocytes.
Consistent with this observation, MCM2 and other MCMs copurified with Pol II and
general transcription factors (GTFs) in high-molecular-weight holoenzyme
complexes isolated from Xenopus oocytes and HeLa cells. Pol II and GTFs also
copurified with MCMs isolated by anti-MCM3 immunoaffinity chromatography. MCMs
were specifically displaced from the holoenzyme complex by antibody against the
C-terminal domain (CTD) of Pol II. In addition, MCMs bound to a CTD affinity
column, suggesting that their association with holoenzyme depends in part on
this domain of Pol II. These results suggest a new function for MCM proteins as
components of the Pol II transcriptional apparatus.

DOI: 10.1128/MCB.19.9.6154
PMCID: PMC84545
PMID: 10454562 [Indexed for MEDLINE]