A globular complex formation by Nda1 and the other five members of the MCM protein family in fission yeast

In the fission yeast Schizosaccharomyces pombe, Nda1, Nda4, Mis5 and Cdc21 proteins belong to the MCM (minichromosome maintenance) protein family which is thought to have six members. Each MCM member is required for the early stages of DNA replication, and has a well‐conserved central 200‐amino acid domain containing a putative ATP binding motif. However, the precise molecular functions of MCM proteins are not yet clear.

[1]  J. Blow,et al.  The RLF‐M component of the replication licensing system forms complexes containing all six MCM/P1 polypeptides , 1997, The EMBO journal.

[2]  H. Nojima,et al.  Licensing of DNA replication by a multi‐protein complex of MCM/P1 proteins in Xenopus eggs , 1997, The EMBO journal.

[3]  T. Okazaki,et al.  Identification of a predominant replication origin in fission yeast. , 1997, Nucleic acids research.

[4]  G. Evan,et al.  Interaction between the Origin Recognition Complex and the Replication Licensing Systemin Xenopus , 1996, Cell.

[5]  T. Coleman,et al.  The Xenopus Cdc6 Protein Is Essential for the Initiation of a Single Round of DNA Replication in Cell-Free Extracts , 1996, Cell.

[6]  R. Laskey,et al.  XMCM7, a novel member of the Xenopus MCM family, interacts with XMCM3 and colocalizes with it throughout replication. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[7]  M. Lei,et al.  Physical interactions among Mcm proteins and effects of Mcm dosage on DNA replication in Saccharomyces cerevisiae , 1996, Molecular and cellular biology.

[8]  J. Usukura,et al.  Demonstration of the Molecular Shape of BP180, a 180-kDa Bullous Pemphigoid Antigen and Its Potential for Trimer Formation* , 1996, The Journal of Biological Chemistry.

[9]  J. Blow,et al.  The role of MCM/P1 proteins in the licensing of DNA replication. , 1996, Trends in biochemical sciences.

[10]  I. Todorov,et al.  The role of MCM proteins in the cell cycle control of genome duplication , 1996, BioEssays : news and reviews in molecular, cellular and developmental biology.

[11]  M. Méchali,et al.  Chromotin binding, nuclear localization and phosphorylation of Xenopus cdc21 are cell‐cycle dependent and associated with the control of initiation of DNA replication. , 1996, The EMBO journal.

[12]  P. O’Farrell,et al.  Drosophila MCM protein complexes. , 1996, Molecular biology of the cell.

[13]  M. Yanagida,et al.  Fission yeast Nda1 and Nda4, MCM homologs required for DNA replication, are constitutive nuclear proteins. , 1996, Journal of cell science.

[14]  Greet Blom van Assendelft,et al.  Fission yeast cdc21, a member of the MCM protein family, is required for onset of S phase and is located in the nucleus throughout the cell cycle. , 1996, The EMBO journal.

[15]  R. Laskey,et al.  Human replication proteins hCdc21, hCdc46 and P1Mcm3 bind chromatin uniformly before S-phase and are displaced locally during DNA replication. , 1996, Journal of cell science.

[16]  Andreas Richter,et al.  Properties of the human nuclear protein p85Mcm. Expression, nuclear localization and interaction with other Mcm proteins. , 1996, European journal of biochemistry.

[17]  Yixian Zheng,et al.  Nucleation of microtubule assembly by a γ-tubulin-containing ring complex , 1995, Nature.

[18]  Z. Kelman,et al.  Protein Structure: Why have six-fold symmetry? , 1995, Current Biology.

[19]  Judith L Campbell,et al.  A yeast gene required for DNA replication encodes a protein with homology to DNA helicases. , 1995, Proceedings of the National Academy of Sciences of the United States of America.

[20]  K. Sugimoto,et al.  Molecular cloning of cDNA encoding mouse Cdc21 and CDC46 homologs and characterization of the products: physical interaction between P1(MCM3) and CDC46 proteins. , 1995, Nucleic acids research.

[21]  A. Attaran,et al.  BM28, a human member of the MCM2-3-5 family, is displaced from chromatin during DNA replication , 1995, The Journal of cell biology.

[22]  R. Knippers,et al.  A human homologue of the yeast replication protein Cdc21. Interactions with other Mcm proteins. , 1995, European journal of biochemistry.

[23]  R. Laskey,et al.  MCM3 complex required for cell cycle regulation of DNA replication in vertebrate cells , 1995, Nature.

[24]  James P. J. Chong,et al.  Purification of an MCM-containing complex as a component of the DNA replication licensing system , 1995, Nature.

[25]  H. Nojima,et al.  Identification of the yeast MCM3-related protein as a component of xenopus DNA replication licensing factor , 1995, Cell.

[26]  P. Springer,et al.  Gene trap tagging of PROLIFERA, an essential MCM2-3-5-like gene in Arabidopsis. , 1995, Science.

[27]  S. Dalton,et al.  Cell cycle-regulated nuclear import and export of Cdc47, a protein essential for initiation of DNA replication in budding yeast. , 1995, Proceedings of the National Academy of Sciences of the United States of America.

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

[29]  B. Alberts,et al.  Nucleation of microtubule assembly by a gamma-tubulin-containing ring complex. , 1995, Nature.

[30]  J. Thompson,et al.  CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. , 1994, Nucleic acids research.

[31]  M. Yanagida,et al.  Fission yeast minichromosome loss mutants mis cause lethal aneuploidy and replication abnormality. , 1994, Molecular biology of the cell.

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

[33]  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.

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

[35]  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.

[36]  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.

[37]  M. Yanagida,et al.  Fission yeast genes nda1+ and nda4+, mutations of which lead to S-phase block, chromatin alteration and Ca2+ suppression, are members of the CDC46/MCM2 family. , 1993, Molecular biology of the cell.

[38]  E V Koonin,et al.  A common set of conserved motifs in a vast variety of putative nucleic acid-dependent ATPases including MCM proteins involved in the initiation of eukaryotic DNA replication. , 1993, Nucleic acids research.

[39]  C. Alfa.  Experiments with fission yeast : a laboratory course manual , 1993 .

[40]  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.

[41]  D. Botstein,et al.  CDC46/MCM5, a yeast protein whose subcellular localization is cell cycle-regulated, is involved in DNA replication at autonomously replicating sequences. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[42]  Qiang Zhou,et al.  Holo-TFIID supports transcriptional stimulation by diverse activators and from a TATA-less promoter. , 1992, Genes & development.

[43]  U. K. Laemmli,et al.  Identification of nuclear pre-replication centers poised for DNA synthesis in Xenopus egg extracts: immunolocalization study of replication protein A , 1992, The Journal of cell biology.

[44]  D. Botstein,et al.  A group of interacting yeast DNA replication genes. , 1991, Genes & development.

[45]  D. Botstein,et al.  Subcellular localization of yeast CDC46 varies with the cell cycle. , 1990, Genes & development.

[46]  N. Tuteja,et al.  A DNA helicase from human cells. , 1990, Nucleic acids research.

[47]  Arthur Kornberg,et al.  A model for initiation at origins of DNA replication , 1988, Cell.

[48]  D. Smith,et al.  Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. , 1988, Gene.

[49]  M. Wigler,et al.  Purification of a RAS-responsive adenylyl cyclase complex from Saccharomyces cerevisiae by use of an epitope addition method , 1988, Molecular and cellular biology.

[50]  J. Blow,et al.  A role for the nuclear envelope in controlling DNA replication within the cell cycle , 1988, Nature.

[51]  L. Montagnier,et al.  Efficiency of poly(A).poly(U) as an adjuvant. , 1988, Immunology today.

[52]  R. Burgess,et al.  Replacement of potassium chloride by potassium glutamate dramatically enhances protein-DNA interactions in vitro. , 1987, Biochemistry.

[53]  M. Rosenberg,et al.  Expression and characterization of the human c-myc DNA-binding protein , 1985, Molecular and cellular biology.

[54]  B. Tye,et al.  Mutants of S. cerevisiae defective in the maintenance of minichromosomes. , 1984, Genetics.

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

[56]  K. Umesono,et al.  Cold-sensitive nuclear division arrest mutants of the fission yeast Schizosaccharomyces pombe. , 1983, Journal of molecular biology.

[57]  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.

[58]  M. M. Bradford.  A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.

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

[60]  K. J. Monty,et al.  Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Application to crude preparations of sulfite and hydroxylamine reductases. , 1966, Biochimica et biophysica acta.