TAILIEUCHUNG - Báo cáo khoa học: Proteolytic processing of porcine deoxyribonuclease II occurs in lysosomes but is not required for enzyme activation

DNase II purified from porcine spleen (pDNase II) comprisesa1, a2 and bsubunits. The three subunits are encoded by one cDNA, in the sequence a1 , b, and a2, and the peptides linking these subunits are presumably cleaved out post-translationally. To understand the relevance of post-trans-lational cleavage to pDNase II, recombinant pDNase II (rpDNase II) was produced in human 293T cells by transfection with an expression plasmid containing pDNase II cDNA (pcDNaseII). | ỊFEBS Journal Proteolytic processing of porcine deoxyribonuclease II occurs in lysosomes but is not required for enzyme activation Ru-Ting Huang Ta-Hsiu Liao and Shao-Chun Lu Department of Biochemistry and Molecular Biology College of Medicine NationalTaiwan University Taipei Taiwan Keywords chloroquine cycloheximide DNase II lysosome post-translationalprocessing Correspondence . Lu Department of Biochemistry and Molecular Biology College of Medicine NationalTaiwan University No. 1 Sec. 1 Jen-Ai Road Taipei Taiwan 10051 Fax. 886 2 2391 5295 Tel. 886 2 2312 3456 ext. 88224 E-mail lsc@ Website http department ibmb english Received 17 December 2008 revised 15 January 2009 accepted 20 January 2009 doi DNase II purified from porcine spleen pDNase II comprises a15 a2 and b subunits. The three subunits are encoded by one cDNA in the sequence a15 b and a2 and the peptides linking these subunits are presumably cleaved out post-translationally. To understand the relevance of post-translational cleavage to pDNase II recombinant pDNase II rpDNase II was produced in human 293T cells by transfection with an expression plasmid containing pDNase II cDNA pcDNaseII . An a 35 and a kDa protein were detected in the cell lysates whereas only a kDa protein was detected in the culture medium of the pcDNaseII-transfected cells. The kDa rpDNase II secreted into the medium was purified to homogeneity and characterized. MALDI-TOF MS and N-terminal amino acid sequencing of the kDa protein revealed a single contiguous polypeptide chain of pDNase II. Zymographic analysis showed that the kDa protein digested DNA in acidic conditions and that the specific activity of this rpDNase II was about twice that of pDNase II purified from porcine spleen. Treatment with chloroquine a lysosomal inhibitor resulted in the accumulation of only the kDa protein in the pcDNaseII-transfected .

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