A new member of the MCM protein family encoded by the human MCM8 gene, located contrapodal to GCD10 at chromosome band 20p12.3-13

被引:55
作者
Johnson, EM
Kinoshita, Y
Daniel, DC
机构
[1] CUNY Mt Sinai Sch Med, Dept Pathol, New York, NY 10029 USA
[2] CUNY Mt Sinai Sch Med, Dept Mol Biol, New York, NY 10029 USA
[3] CUNY Mt Sinai Sch Med, DH Ruttenberg Canc Ctr, New York, NY 10029 USA
关键词
D O I
10.1093/nar/gkg395
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The MCM8 protein from HeLa cells, a new member of the MCM family, co-isolates through several steps with MCM6 and MCM7, and MCM8 co-immunoprecipitates with MCM4, MCM6 and MCM7, proteins reportedly forming a helicase complex involved in initiation of DNA replication. MCM8 mRNA is expressed in placenta, lung and liver, but is also significantly expressed in adult heart, a tissue with a low percentage of proliferating cells. The MCM8 gene, consisting of 19 exons, is located contrapodal to a gene, consisting of 11 exons, encoding a homolog of the yeast GCD10 gene product. The region between these two transcription units, comprising as few as 62 bp, is TATA-less and highly GC-rich, containing multiple CpG units. MCM8 expression is altered in certain forms of neoplasia. In a case of choriocarcinoma MCM8 mRNA is aberrant, leading to expression of a protein lacking 16 amino acids. In several cases of colon adenocarcinoma MCM8 expression is greatly reduced relative to matched non-cancerous tissue. The potential helicase domain of MCM8 is different from those of other MCM proteins in that it is more homologous to canonical ATP-binding domains of other known helicases. Results suggest that MCM8 may interact with other MCM proteins to alter the function of the replicative MCM protein complex.
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页码:2915 / 2925
页数:11
相关论文
共 35 条
[1]  
ALTSCHUL SF, 1990, J MOL BIOL, V215, P403, DOI 10.1006/jmbi.1990.9999
[2]   Bidirectional promoter connects the poly(ADP-ribose) polymerase 2 (PARP-2) gene to the gene for RNase P RNA -: Structure and expression of the mouse PARP-2 gene [J].
Amé, JC ;
Schreiber, V ;
Fraulob, V ;
Dollé, P ;
de Murcia, G ;
Niedergang, CP .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (14) :11092-11099
[3]   The Gcd10p/Gcd14p complex is the essential two-subunit tRNA(1-methyladenosine) methyltransferase of Saccharomyces cerevisiae [J].
Anderson, J ;
Phan, L ;
Hinnebusch, AG .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (10) :5173-5178
[4]   Ras-induced colony formation and anchorage-independent growth inhibited by elevated expression of Purα in NIH3T3 cells [J].
Barr, SM ;
Johnson, EM .
JOURNAL OF CELLULAR BIOCHEMISTRY, 2001, 81 (04) :621-638
[5]   DNA replication in eukaryotic cells [J].
Bell, SP ;
Dutta, A .
ANNUAL REVIEW OF BIOCHEMISTRY, 2002, 71 :333-374
[6]   CPG-RICH ISLANDS AND THE FUNCTION OF DNA METHYLATION [J].
BIRD, AP .
NATURE, 1986, 321 (6067) :209-213
[7]   PURIFICATION OF AN MCM-CONTAINING COMPLEXES A COMPONENT OF THE DNA-REPLICATION LICENSING SYSTEM [J].
CHONG, JPJ ;
MAHBUBANI, HM ;
KHOO, CY ;
BLOW, JJ .
NATURE, 1995, 375 (6530) :418-421
[8]   MULTIPLE SEQUENCE ALIGNMENT WITH HIERARCHICAL-CLUSTERING [J].
CORPET, F .
NUCLEIC ACIDS RESEARCH, 1988, 16 (22) :10881-10890
[9]  
Daniel DC, 1999, CELL TISSUE RES, V298, P481, DOI 10.1007/s004410050070
[10]   Highlight: BRCA1 and BRCA2 proteins in breast cancer [J].
Daniel, DC .
MICROSCOPY RESEARCH AND TECHNIQUE, 2002, 59 (01) :68-83