Characterization of a telomere-binding protein from Physarum polycephalum.

Abstract:

:We have partially purified a nuclear protein (PPT) from Physarum polycephalum that binds to the extrachromosomal ribosomal DNA telomeres of this acellular slime mold. Binding is specific for the (T2AG3)n telomere repeats, as evidenced by nitrocellulose filter binding assays, by gel mobility shift assays with both DNA fragments and double-stranded oligonucleotides, and by DNase I footprinting. PPT is remarkably heat stable, showing undiminished binding activity after incubation at 90 degrees C. It sediments at 1.2S, corresponding to a molecular weight of about 10,000 (for a globular protein), and its binding activity is undiminished by incubation with RNase, suggesting that it is not a ribonucleoprotein. We hypothesize that PPT plays a structural role in telomeres, perhaps preventing nucleolytic degradation or promoting telomere extension by a telomere-specific terminal transferase.

journal_name

Mol Cell Biol

authors

Coren JS,Epstein EM,Vogt VM

doi

10.1128/mcb.11.4.2282

subject

Has Abstract

pub_date

1991-04-01 00:00:00

pages

2282-90

issue

4

eissn

0270-7306

issn

1098-5549

journal_volume

11

pub_type

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