Biology in pictures. New light on sticky sisters

Losada, A., Hirano, T. (September 2000) Biology in pictures. New light on sticky sisters. Curr Biol, 10 (17). R615. ISSN 0960-9822 (Print)

URL: http://www.ncbi.nlm.nih.gov/pubmed/10996082
DOI: 10.1016/S0960-9822(00)00670-9

Abstract

Cohesin, a multisubunit protein complex conserved from yeast to humans, plays a major role in sister chromatid cohesion. In Saccharomyces cerevisiae, cohesins bind to chromatin before or during DNA replication and remain bound until the metaphase–anaphase transition. In vertebrate cells, however, most cohesins dissociate from chromatin in early mitosis, long before the onset of anaphase. This is clearly shown in the picture above where two Chinese hamster ovary (CHO) cells, one in interphase (top) and one in metaphase (bottom), are stained with a DNA-binding dye (red) and an antibody against XSA1 (green), a recently identified subunit of vertebrate cohesin complexes

Item Type: Paper
Uncontrolled Keywords: Animals CHO Cells Cell Cycle Proteins Chromosomal Proteins, Non-Histone Chromosomes Cricetinae Fungal Proteins Nuclear Proteins/ ultrastructure Saccharomyces cerevisiae/genetics/metabolism Xenopus
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification
organs, tissues, organelles, cell types and functions > cell types and functions > cell functions > cell cycle
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > Chromatin dynamics
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > cohesin
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > cohesin complex
organism description > yeast
CSHL Authors:
Communities: CSHL labs > Hirano lab
Depositing User: Matt Covey
Date: 7 September 2000
Date Deposited: 31 Jan 2014 16:27
Last Modified: 31 Jan 2014 16:27
Related URLs:
URI: https://repository.cshl.edu/id/eprint/29359

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