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Linda J. Palmisano(1), Cristy L. Gelling(1), Geoffrey
Kornfeld(2), Ian W. Dawes(2). (1) School of Biotech & Biomol Sci,
University of New South Wales, Sydney, New South Wales, 2052,
Australia; (2) Ramaciotti Centre for Gene Function Analysis and
School of Biotech & Biomol Sci, University of NSW, Sydney, NSW,
2052, Australia.
During its lifespan each nuclear eukaryotic transcript will undergo
a number of steps at which it may be processed in a variety of
different ways. A number of mechanisms have been identified which
allow the cell to vary the manner in which these
post-transcriptional modifications are carried out, with potentially
profound effects on the amount of protein produced in each case.
This study examines the modulation of splicing as a possible
additional level of post-transcriptional regulation in the model
eukaryote, S. cerevisiae, and investigates the manner in which such
regulation may be achieved. Spliceosomal Lsm proteins form part of
an ancient family stretching back into Archaea and have been
implicated in an increasing number of key RNA modification complexes
in the eukaryotic cell. We studied the regulation of the Lsm
proteins under a variety of metabolic conditions and examined the
resulting patterns for correlation with both the splicing
requirements of the cell and the amount of splicing occurring in
vivo under these conditions, using a novel in vivo splicing assay.
Interestingly two of the LSM genes encoding spliceosomal proteins
contain introns themselves, and the extent to which these contribute
to autoregulation of these genes, and their influence on the
regulation of other elements of the spliceosomal complex have been
explored.
Program Nr. 404B from 2004 Yeast meeting |
