A human homologue of the yeast replication protein Cdc21. Interactions with other Mcm proteins.

We present the amino acid sequence of the human homologue of the yeast replication protein Cdc21, a member of the Mcm family of nuclear proteins. Specific antibodies, raised against protein hCdc21, were used to investigate the expression of the protein through the cell cycle. The protein is highly phosphorylated in mitotic cells. The phosphorylated form of protein hCdc21 appears to be less tightly bound to nuclear structures than the underphosphorylated form suggesting that phosphorylation/dephosphorylation reactions may determine the nuclear distribution of the protein. Protein hCdc21 forms a stable trimeric complex with two novel human Mcm proteins, p85Mcm and p105Mcm. Protein BM28/Mcm2 is more loosely associated with the trimeric hCdc21 complex.

[1]  H. Hameister,et al.  Expression, phosphorylation and nuclear localization of the human P1 protein, a homologue of the yeast Mcm 3 replication protein. , 1995, Journal of cell science.

[2]  R. Knippers,et al.  Interactions of human nuclear proteins P1Mcm3 and P1Cdc46. , 1995, European journal of biochemistry.

[3]  L. Johnston,et al.  The activation of DNA replication in yeast. , 1995, Trends in biochemical sciences.

[4]  Y. Nakamura,et al.  Isolation and mapping of a human gene (MCM2) encoding a product homologous to yeast proteins involved in DNA replication. , 1995, Cytogenetics and cell genetics.

[5]  S. Forsburg,et al.  The fission yeast cdc19+ gene encodes a member of the MCM family of replication proteins. , 1994, Journal of cell science.

[6]  K. Sugimoto,et al.  DNA polymerase alpha associated protein P1, a murine homolog of yeast MCM3, changes its intranuclear distribution during the DNA synthetic period. , 1994, The EMBO journal.

[7]  B. Tye.  The MCM2-3-5 proteins: are they replication licensing factors? , 1994, Trends in cell biology.

[8]  R. Pepperkok,et al.  A human nuclear protein with sequence homology to a family of early S phase proteins is required for entry into S phase and for cell division. , 1994, Journal of cell science.

[9]  R. Knippers,et al.  The P1 family: a new class of nuclear mammalian proteins related to the yeast Mcm replication proteins. , 1993, Nucleic acids research.

[10]  B. Tye,et al.  Cell cycle-regulated nuclear localization of MCM2 and MCM3, which are required for the initiation of DNA synthesis at chromosomal replication origins in yeast. , 1993, Genes & development.

[11]  Erich A. Nigg,et al.  Cellular substrates of p34cdc2 and its companion cyclin-dependent kinases , 1993 .

[12]  M. Jacquet,et al.  A 12·8 kb segment, on the right arm of chromosome II from Saccharomyces cerevisiae including part of the DUR1, 2 gene, contains five putative new genes , 1993, Yeast.

[13]  A. Coxon,et al.  Fission yeast cdc21+ belongs to a family of proteins involved in an early step of chromosome replication. , 1992, Nucleic acids research.

[14]  S. Adam,et al.  Nuclear protein import using digitonin-permeabilized cells. , 1992, Methods in enzymology.

[15]  M. Kozak,et al.  An analysis of vertebrate mRNA sequences: intimations of translational control , 1991, The Journal of cell biology.

[16]  B. Tye,et al.  Mcm2 and Mcm3, two proteins important for ARS activity, are related in structure and function. , 1991, Genes & development.

[17]  R. Laskey,et al.  Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: Identification of a class of bipartite nuclear targeting sequence , 1991, Cell.

[18]  B. Tye,et al.  The phenotype of the minichromosome maintenance mutant mcm3 is characteristic of mutants defective in DNA replication , 1990, Molecular and cellular biology.

[19]  B. Kemp,et al.  Protein kinase recognition sequence motifs. , 1990, Trends in biochemical sciences.

[20]  J. Sambrook,et al.  Molecular Cloning: A Laboratory Manual , 2001 .

[21]  H. Towbin,et al.  Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. , 1979, Proceedings of the National Academy of Sciences of the United States of America.

[22]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.