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PMID: 2005910 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Characterization of a telomere-binding protein from Physarum polycephalum.

Molecular and cellular biology ·Vol. 11 ·No. 4 ·1991-04-00 ·Pages 2282-90

Coren JS, Epstein EM, Vogt VM

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.

MeSH Terms
Base Sequence Chromosomes, Fungal/metabolism DNA-Binding Proteins/chemistry,isolation & purification,metabolism Deoxyribonuclease I/metabolism Electrophoresis, Polyacrylamide Gel Fungal Proteins/chemistry,isolation & purification,metabolism Molecular Sequence Data Molecular Weight Physarum/metabolism Repetitive Sequences, Nucleic Acid
Chemicals
DNA-Binding Proteins Fungal Proteins Deoxyribonuclease I
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Coren J S
Section of Genetics and Development, Cornell University, Ithaca, New York 14853.
Epstein E M
Vogt V M
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
Published
1991-04-00
Pages
2282-90
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC359930
Subset
IM
Grants
NIGMS NIH HHS · GM 31577 · United States
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