We have taken advantage of the synchrony of meiotic prophase I in Lilium microsporocytes to investigate the presence and involvement in four stages of meiotic prophase I (leptotene, zygotene, pachytene, and diplotene) of the p34 H1 histone kinase, a component of MPF and a key participant in division control in other eukaryotes. H1 kinase activity showed a peak pattern during meiotic prophase I with the highest kinase activity at pachytene. A monoclonal antibody directed against a highly conserved region of p34 (termed the 'PSTAIR') recognized three major protein forms by immunoblotting. The highest level of the fastest-migrating form was observed at pachytene, coinciding with the highest activity of H1 kinase. Both the proteins recognized by the anti-PSTAIR antibody and H1 histone kinase activity were retained on beads conjugated with p13 , a protein known to physically associate with p34 . These observations suggest that p34 or protein(s) highly homologous to p34 is a component of Lilium H1 histone kinase and plays a role in regulating meiotic prophase I.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1111/j.1440-169X.1991.00625.x | DOI Listing |
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!