FUNCTIONAL DOMAINS OF NUCLEOLAR PHOSPHOPROTEIN P120

Citation
E. Durban et al., FUNCTIONAL DOMAINS OF NUCLEOLAR PHOSPHOPROTEIN P120, Physiological chemistry and physics and medical NMR, 27(4), 1995, pp. 303-311
Citations number
26
Categorie Soggetti
Biophysics,Biology,Physiology,"Radiology,Nuclear Medicine & Medical Imaging
ISSN journal
07486642
Volume
27
Issue
4
Year of publication
1995
Pages
303 - 311
Database
ISI
SICI code
0748-6642(1995)27:4<303:FDONPP>2.0.ZU;2-Q
Abstract
Nucleolar phosphoprotein p120 is a low abundance, proliferation-associ ated protein. Several functional domains have been characterized and a re discussed here such as the antigenic domain recognized by a monoclo nal antibody, the nuclear/nucleolar localization domain, phosphorylati on domains of casein kinase II (CKII) and protein kinase C, a putative methylation domain and an RNA binding region. By sucrose gradient sed imentation analyses, protein p120 was shown to rapidly sediment with 6 0-80 S pre-rRNP particles but sedimented more slowly when treated with RNAse or salt suggesting binding to RNA. Nucleolar protein p 120 diff ered from other nucleolar proteins such as C23 (nucleolin) and B23 (nu cleophosmin) which sedimented more slowly near the top of the gradient .