Phosphorylated proteins are involved in sister-chromatid arm cohesion during meiosis I.
Sister-chromatid arm cohesion is lost during the metaphase I/anaphase I transition to allow homologue separation. To obtain needed information on this process we have analysed in grasshopper bivalents the sequential release of arm cohesion in relation to the behaviour of chromatid axes. Results show that sister axes are associated during early metaphase I but separate during late metaphase I leading to a concomitant change of chromosome structure that implies the loss of sister-kinetochore cohesion. Afterwards, homologues initiate their separation asynchronously depending on their size, and number and position of chiasmata. In all bivalents thin chromatin strands at the telomeres appeared as the last point of contact between sister chromatids. Additionally, we have analysed the participation of phosphoproteins recognised by the MPM-2 monoclonal antibody against mitotic phosphoproteins in arm cohesion in bivalents and two different kinds of univalents. Results show the absence of MPM-2 phosphoproteins at the interchromatid domain in mitotic chromosomes and meiotic univalents, but their presence in metaphase I bivalents. These phosphoproteins are lost at the onset of anaphase I. Taken together, these data have prompted us to propose a 'working' model for the release of arm cohesion during meiosis I. The model suggests that MPM-2 phosphoproteins may act as cohesive proteins associating sister axes. Their modification, once all bivalents are correctly aligned at the metaphase plate, would trigger a change of chromosome structure and the sequential release of sister-kinetochore, arm, and telomere cohesions.
Suja
J A
JA
Unidad de Biología Celular, Departamento de Biología, Facultad de Ciencias, Universidad Autónoma, E-28049 Madrid, Spain. jose.suja@uam.es
Antonio
C
C
Debec
A
A
Rufas
J S
JS
D000705:Anaphase; D000818:Animals; D002842:Chromatids / Q000648:ultrastructure; D006110:Grasshoppers; D019476:Insect Proteins / Q000502:physiology*; D018386:Kinetochores / Q000502:physiology; D008297:Male; D008540:Meiosis / Q000502:physiology*; D008677:Metaphase; D008854:Microscopy, Electron; D008856:Microscopy, Fluorescence; D010750:Phosphoproteins / Q000502:physiology*; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D016622:Silver Staining; D012854:Sister Chromatid Exchange / Q000502:physiology*; D013090:Spermatocytes / Q000648:ultrastructure*; D016615:Telomere / Q000502:physiology / Q000648:ultrastructure
D019476:Insect Proteins; D010750:Phosphoproteins; D017346:Protein Serine-Threonine Kinases