---
pmid: '12392551'
title: Distinct parts of minichromosome maintenance protein 2 associate with histone
  H3/H4 and RNA polymerase II holoenzyme.
authors:
- Holland L
- Gauthier L
- Bell-Rogers P
- Yankulov K
journal: Eur J Biochem
year: '2002'
full_text_available: false
doi: 10.1046/j.1432-1033.2002.03224.x
pubmed_publication_types:
- Journal Article
- Research Support, Non-U.S. Gov't
publication_type: PRIMARY_RESEARCH
---

# Distinct parts of minichromosome maintenance protein 2 associate with histone H3/H4 and RNA polymerase II holoenzyme.
**Authors:** Holland L, Gauthier L, Bell-Rogers P, Yankulov K
**Journal:** Eur J Biochem (2002)
**DOI:** [10.1046/j.1432-1033.2002.03224.x](https://doi.org/10.1046/j.1432-1033.2002.03224.x)

## Abstract

1. Eur J Biochem. 2002 Nov;269(21):5192-202. doi:
10.1046/j.1432-1033.2002.03224.x.

Distinct parts of minichromosome maintenance protein 2 associate with histone
H3/H4 and RNA polymerase II holoenzyme.

Holland L(1), Gauthier L, Bell-Rogers P, Yankulov K.

Author information:
(1)Department of Molecular Biology and Genetics, University of Guelph, Ontario
Canada.

Minichromosome maintenance (MCM) proteins are part of the replication licensing
factor (RLF-M), which limits the initiation of DNA replication to once per cell
cycle. We have previously reported that higher order complexes of mammalian pol
II and general pol II transcription factors, referred to as pol II holoenzyme,
also contain MCM proteins. In the present study we have analyzed in detail the
interaction between MCM2 and pol II holoenzyme. N- and C- terminal deletions
were introduced into epitope-tagged MCM2 and the truncated proteins were
transiently expressed in 293 cells. Affinity chromatography was used to purify
RNA pol II holoenzyme and histone binding MCM complexes. We found that amino
acids 168-230 of MCM2 are required for its binding to pol II holoenzyme in vivo.
We also showed that bacterially expressed amino acids 169-212 of MCM2 associate
with pol II and several general transcription factors in vitro. Point mutations
within the 169-212 domain of MCM2 disrupted its interaction with pol II
holoenzyme both in vitro and in vivo. This region is distinct from the
previously characterized histone H3 binding domain of MCM2.

DOI: 10.1046/j.1432-1033.2002.03224.x
PMID: 12392551 [Indexed for MEDLINE]