Kim, Yun-Kyoung Lee, Won Kyu Jin, Youngnam Lee, Kong-Joo Jeon, Hyesung Yu, Yeon Gyu 2024-01-21T02:03:14Z 2024-01-21T02:03:14Z 2022-01-10 2006-11-30 1225-8687 https://pubs.kist.re.kr/handle/201004/134945 Human nucleolar phosphoprotein p140 (hNopp140) is a nucleolar phosphoprotein that can bind to doxorubicin, an anti-cancer agent. We have examined the interaction between hNopp140 and doxorubicin as well as the folding property of hNopp140. Also, the effects of ATP and phosphorylation on the affinity of hNopp140 to doxorubicin are investigated by affinity dependent co-precipitation and surface plasmon resonance methods. Doxorubicin preferentially binds to un-phosphorylated form of hNopp140 with a Ko value of 3.3 X 10(-7) M. Furthermore, doxorubicin reduces the protein kinase CK2-dependent phosphorylation of hNopp140, indicating that doxorubicin may perturb the cellular function of hNopp140 by reducing the protein kinase CK2-dependent phosphorylation of hNopp140. Low contents of the secondary structures of hNopp140 and the fast rate of proteolysis imply that hNopp140 has a high percentage of flexible regions or extended loop structures. English SPRINGER SINGAPORE PTE LTD NUCLEOLAR PHOSPHOPROTEIN P130 SMOOTH-MUSCLE CALDESMON SECONDARY STRUCTURE ESCHERICHIA-COLI CROSS-LINKING CELL-CYCLE NOPP140 PURIFICATION ADRIAMYCIN EXPRESSION Doxorubicin binds to un-phosphorylated form of hNopp140 and reduces protein kinase CK2-dependent phosphorylation of hNopp140 Article 1 JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY, v.39, no.6, pp.774 - 781 JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY 39 6 774 781 scie scopus kci ART001031209 000242360600018 2-s2.0-33845420057 Biochemistry & Molecular Biology Biochemistry & Molecular Biology Article NUCLEOLAR PHOSPHOPROTEIN P130 SMOOTH-MUSCLE CALDESMON SECONDARY STRUCTURE ESCHERICHIA-COLI CROSS-LINKING CELL-CYCLE NOPP140 PURIFICATION ADRIAMYCIN EXPRESSION doxorubicin hNopp140 phosphorylation protein kinase CK2