Nucleic Acids Research, Vol 24, Issue 15 3023-3030, Copyright © 1996 by Oxford University Press
X Liu and MA Gorovsky
A truncated cDNA clone encoding Tetrahymena thermophila histone H2A2 was
isolated using synthetic degenerate oligonucleotide probes derived from H2A
protein sequences of Tetrahymena pyriformis. The cDNA clone was used as a
homologous probe to isolate a truncated genomic clone encoding H2A1. The
remaining regions of the genes for H2A1 (HTA1) and H2A2 (HTA2) were then
isolated using inverse PCR on circularized genomic DNA fragments. These
partial clones were assembled into intact HTA1 and HTA2 clones. Nucleotide
sequences of the two genes were highly homologous within the coding region
but not in the noncoding regions. Comparison of the deduced amino acid
sequences with protein sequences of T. pyriformis H2As showed only two and
three differences respectively, in a total of 137 amino acids for H2A1, and
132 amino acids for H2A2, indicating the two genes arose before the
divergence of these two species. The HTA2 gene contains a TAA triplet
within the coding region, encoding a glutamine residue. In contrast with
the T. thermophila HHO and HTA3 genes, no introns were identified within
the two genes. The 5'- and 3'-ends of the histone H2A mRNAs; were
determined by RNase protection and by PCR mapping using RACE and RLM- RACE
methods. Both genes encode polyadenylated mRNAs and are highly expressed in
vegetatively growing cells but only weakly expressed in starved cultures.
With the inclusion of these two genes, T. thermophila is the first organism
whose entire complement of known core and linker histones, including
replication-dependent and basal variants, has been cloned and sequenced.
ARTICLES
Cloning and characterization of the major histone H2A genes completes the cloning and sequencing of known histone genes of Tetrahymena thermophila
Department of Biology, University of Rochester, NY 14627, USA.
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