Nucleic Acids Research, Vol 27, Issue 24 4687-4694, Copyright © 1999 by Oxford University Press
NS Vassetzky, F Gaden, C Brun, SM Gasser and E Gilson
Band shift assays were used to study proteins from the fission yeast that
bind double-stranded telomeric repeat sequences. We also examine general
DNA binding properties of the telobox domain, which characterizes
telomere-binding proteins from a range of species. We demonstrate that
Taz1p has a high affinity for the fission yeast telomeric repeat,
consistent with genetic results implicating this protein in telomere
maintenance. A second Schizosaccharomyces pombe telobox protein, Teb1p, is
shown to bind with high affinity to the vertebrate repeat and with low
affinity to the fission yeast telomeric DNA. When tested on G-rich
single-stranded telomeric DNA, all these proteins bind with very low
affinity, much like the human telomere- binding protein TRF1. Recombinant
proteins containing just the telobox domains reproduce the specificity of
binding demonstrated for the corresponding full-length proteins, indicating
that the telobox domain is indeed responsible for specific DNA recognition.
The presence of possible Teb1p-binding sites upstream of many genes
suggests a role for this protein as a general transcription factor.
Finally, band shift experiments with whole cell extracts from wild-type and
taz1 (-)strains suggest that in addition to Taz1p, S.pombe has another
major telomere- binding activity.
ARTICLES
Taz1p and Teb1p, two telobox proteins in Schizosaccharomyces pombe, recognize different telomere-related DNA sequences
Engelhardt Institute of Molecular Biology, 32 Vavilov Street, Moscow, 117984 Russia,
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