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 Bioljournal_title
Molecular and cellular biologyauthors
Coren JS,Epstein EM,Vogt VMdoi
10.1128/mcb.11.4.2282subject
Has Abstractpub_date
1991-04-01 00:00:00pages
2282-90issue
4eissn
0270-7306issn
1098-5549journal_volume
11pub_type
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