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      The Ndc80p Complex from Saccharomyces cerevisiae Contains Conserved Centromere Components and Has a Function in Chromosome Segregation

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      Author(s): a , a
      Publication date (Print):
      Journal: The Journal of Cell Biology
      Publisher: The Rockefeller University Press
      Keywords: Ndc80p, Nuf2p, Spc25p, Spc24p, centromere

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          Abstract

          We have purified a complex from Saccharomyces cerevisiae containing the spindle components Ndc80p, Nuf2p, Spc25p, and Spc24p. Temperature-sensitive mutants in NDC80, SPC25, and SPC24 show defects in chromosome segregation. In spc24-1 cells, green fluorescence protein (GFP)-labeled centromeres fail to split during spindle elongation, and in addition some centromeres may detach from the spindle. Chromatin immunoprecipitation assays show an association of all four components of the complex with the yeast centromere. Homologues of Ndc80p, Nuf2p, and Spc24p were found in Schizosaccharomyces pombe and GFP tagging showed they were located at the centromere. A human homologue of Nuf2p was identified in the expressed sequence tag database. Immunofluorescent staining with anti–human Nuf2p and with anti-HEC, the human homologue of Ndc80p, showed that both proteins are at the centromeres of mitotic HeLa cells. Thus the Ndc80p complex contains centromere-associated components conserved between yeasts and vertebrates.

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          A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae.

          Peter Uetz, Loic Giot, Gerard Cagney … (2000)
          Two large-scale yeast two-hybrid screens were undertaken to identify protein-protein interactions between full-length open reading frames predicted from the Saccharomyces cerevisiae genome sequence. In one approach, we constructed a protein array of about 6,000 yeast transformants, with each transformant expressing one of the open reading frames as a fusion to an activation domain. This array was screened by a simple and automated procedure for 192 yeast proteins, with positive responses identified by their positions in the array. In a second approach, we pooled cells expressing one of about 6,000 activation domain fusions to generate a library. We used a high-throughput screening procedure to screen nearly all of the 6,000 predicted yeast proteins, expressed as Gal4 DNA-binding domain fusion proteins, against the library, and characterized positives by sequence analysis. These approaches resulted in the detection of 957 putative interactions involving 1,004 S. cerevisiae proteins. These data reveal interactions that place functionally unclassified proteins in a biological context, interactions between proteins involved in the same biological function, and interactions that link biological functions together into larger cellular processes. The results of these screens are shown here.
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            Improved tools for biological sequence comparison.

            W R Pearson, D J Lipman (1988)
            We have developed three computer programs for comparisons of protein and DNA sequences. They can be used to search sequence data bases, evaluate similarity scores, and identify periodic structures based on local sequence similarity. The FASTA program is a more sensitive derivative of the FASTP program, which can be used to search protein or DNA sequence data bases and can compare a protein sequence to a DNA sequence data base by translating the DNA data base as it is searched. FASTA includes an additional step in the calculation of the initial pairwise similarity score that allows multiple regions of similarity to be joined to increase the score of related sequences. The RDF2 program can be used to evaluate the significance of similarity scores using a shuffling method that preserves local sequence composition. The LFASTA program can display all the regions of local similarity between two sequences with scores greater than a threshold, using the same scoring parameters and a similar alignment algorithm; these local similarities can be displayed as a "graphic matrix" plot or as individual alignments. In addition, these programs have been generalized to allow comparison of DNA or protein sequences based on a variety of alternative scoring matrices.
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              A central role for cohesins in sister chromatid cohesion, formation of axial elements, and recombination during yeast meiosis.

              F. Klein, P Mahr, M Gálová … (1999)
              A multisubunit complex, called cohesin, containing Smc1p, Smc3p, Scc1p, and Scc3p, is required for sister chromatid cohesion in mitotic cells. We show here that Smc3p and a meiotic version of Scc1p called Rec8p are required for cohesion between sister chromatids, for formation of axial elements, for reciprocal recombination, and for preventing hyperresection of double-strand breaks during meiosis. Both Rec8p and Smc3p colocalize with chromosome cores independently of synapsis during prophase I and largely disappear from chromosome arms after pachytene but persist in the neighborhood of centromeres until the onset of anaphase II. The eukaryotic cell's cohesion apparatus is required both for the repair of recombinogenic lesions and for chromosome segregation and therefore appears to lie at the heart of the meiotic process.
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                Author and article information

                Contributors
                :
                MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.44-1223-412-14244-1223-402-242
                Journal
                Journal ID (nlm-ta): J Cell Biol
                Title: The Journal of Cell Biology
                Publisher: The Rockefeller University Press
                ISSN (Print): 0021-9525
                ISSN (Electronic): 1540-8140
                Publication date (Print): 22 January 2001
                Volume: 152
                Issue: 2
                Pages: 349-360
                Affiliations
                [a ]Medical Research Council, Laboratory of Molecular Biology, Cambridge CB2 2QH, United Kingdom
                Article
                Publisher ID: 0011039
                DOI: 10.1083/jcb.152.2.349
                PMC ID: 2199619
                PubMed ID: 11266451
                SO-VID: 56354013-c5e9-4d2b-b5a5-4a70938de479
                Copyright © © 2001 The Rockefeller University Press
                History
                Date received : 8 November 2000
                Date revision requested : 6 December 2000
                Date accepted : 8 December 2000
                Categories
                Subject: Original Article

                ScienceOpen disciplines: Cell biology
                Keywords: spc24p,spc25p,centromere,ndc80p,nuf2p
                Data availability:
                ScienceOpen disciplines: Cell biology
                Keywords: spc24p, spc25p, centromere, ndc80p, nuf2p

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