Kim, YK Jin, YN Vukoti, KM Park, JK Kim, EE Lee, KJ Yu, YG 2024-01-21T08:10:13Z 2024-01-21T08:10:13Z 2021-09-03 2003-10 1046-5928 https://pubs.kist.re.kr/handle/201004/138215 Human nucleolar phosphoprotein 140, hNopp140, is one of the most highly phosphorylated mammalian proteins, which is involved in the biogenesis of nucleolus. It regulates the transcription of rDNA and has a tendency to bind to doxorubicin, which is widely used as an anti-cancer drug. The biochemical and biophysical property of hNopp140 has not been reported due to the fact that it is rather difficult to obtain protein in large enough quantity. In this paper, we report the cloning and overexpression of the soluble form of hNopp140 in Escherichia coli. The protein was purified to more than 90% homogeneity using hydroxyapatite and ion exchange chromatography. The purified protein can be extensively phosphorylated by casein kinase II and oligomerized into an insoluble aggregate in the presence of magnesium, carbonate, and fluoride ions. (C) 2003 Elsevier Inc. All rights reserved. English ACADEMIC PRESS INC ELSEVIER SCIENCE COILED BODIES NOPP140 PROTEIN P130 IDENTIFICATION TRANSCRIPTION COMPLEXES Purification and characterization of human nucleolar phosphoprotein 140 expressed in Escherichia coli Article 10.1016/S1046-5928(03)00194-3 1 PROTEIN EXPRESSION AND PURIFICATION, v.31, no.2, pp.260 - 264 PROTEIN EXPRESSION AND PURIFICATION 31 2 260 264 scie scopus 000185977000013 2-s2.0-0142183554 Biochemical Research Methods Biochemistry & Molecular Biology Biotechnology & Applied Microbiology Biochemistry & Molecular Biology Biotechnology & Applied Microbiology Article COILED BODIES NOPP140 PROTEIN P130 IDENTIFICATION TRANSCRIPTION COMPLEXES Escherichia coli