Nucleic Acids Research, Vol 27, Issue 11 2393-2399, Copyright © 1999 by Oxford University Press
J Brzeski, W Podstolski, K Olczak and A Jerzmanowski
The multiprotein complexes involved in active dis-ruption of chromatin
structure, homologous to yeast SWI/SNF complex, have been described for
human and Drosophila cells. In all SWI/SNF-class complexes characterised so
far, one of the key components is the SNF5-type protein. Here we describe
the isolation of a plant (Arabidopsis thaliana ) cDNA encoding a 27 kDa
protein which we named BSH, with high homology to yeast SNF5p and its human
(INI1) and Drosophila (SNR1) counterparts as well as to other putative
SNF5-type proteins from Caenorhabditis elegans, fish and yeast. With 240
amino acids, the Arabidopsis BSH is the smallest SNF5-type protein so far
identified. When expressed in Saccharomyces cerevisiae, the gene for BSH
partially complements the snf5 mutation. BSH is, however, unable to
activate transcription in yeast when tethered to DNA. The gene for BSH
occurs in single copy in the Arabidopsis genome and is ubiquitously
expressed in the plant. Analysis of the whole cell and nuclear protein
extracts with antibodies against recombinant BSH indicates that the protein
is localised in nuclei. Transgenic Arabidopsis plants with markedly
decreased physiological level of the BSH mRNA, resulting from the
expression of antisense messenger, are viable but exhibit a distinctive
phenotype characterised by bushy growth and flowers that are unable to
produce seeds.
ARTICLES
Identification and analysis of the Arabidopsis thaliana BSH gene, a member of the SNF5 gene family
Institute of Biochemistry and Biophysics, Polish Academy of Sciences and Laboratory of Plant Molecular Biology, Warsaw University, Pawinskiego 5A, 02-106 Warsaw, Poland.
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