cDNA cloning of human DNA topoisomerase I: catalytic activity of a 67.7-kDa carboxyl-terminal fragment. Export

@article{citeulike:3740815, abstract = {cDNA clones encoding human topoisomerase I were isolated from an expression vector library (lambda gt11) screened with autoimmune anti-topoisomerase I serum. One of these clones has been expressed as a fusion protein comprised of a 32-kDa fragment of the bacterial TrpE protein linked to 67.7 kDa of protein encoded by the cDNA. Three lines of evidence indicate that the cloned cDNA encodes topoisomerase I. (i) Proteolysis maps of the fusion protein and human nuclear topoisomerase I are essentially identical. (ii) The fusion protein relaxes supercoiled DNA, an activity that can be immunoprecipitated by anti-topoisomerase I serum. (iii) Sequence analysis has revealed that the longest cDNA clone (3645 base pairs) encodes a protein of 765 amino acids that shares 42\% identity with Saccharomyces cerevisiae topoisomerase I. The sequence data also show that the catalytically active 67.7-kDa fragment is comprised of the carboxyl terminus.}, address = {Department of Cell Biology and Anatomy, Johns Hopkins University School of Medicine, Baltimore, MD 21205.}, author = {D'Arpa, P. and Machlin, P. S. and Ratrie, H. and Rothfield, N. F. and Cleveland, D. W. and Earnshaw, W. C.}, citeulike-article-id = {3740815}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/2833744}, journal = {Proceedings of the National Academy of Sciences of the United States of America}, keywords = {coletta, gene, topoisomerase}, month = {April}, number = {8}, pages = {2543--2547}, posted-at = {2008-12-03 15:12:12}, priority = {2}, title = {cDNA cloning of human DNA topoisomerase I: catalytic activity of a 67.7-kDa carboxyl-terminal fragment.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/2833744}, volume = {85}, year = {1988} }

TY - JOUR ID - citeulike:3740815 L3 - citeulike-article-id:3740815 N2 - cDNA clones encoding human topoisomerase I were isolated from an expression vector library (lambda gt11) screened with autoimmune anti-topoisomerase I serum. One of these clones has been expressed as a fusion protein comprised of a 32-kDa fragment of the bacterial TrpE protein linked to 67.7 kDa of protein encoded by the cDNA. Three lines of evidence indicate that the cloned cDNA encodes topoisomerase I. (i) Proteolysis maps of the fusion protein and human nuclear topoisomerase I are essentially identical. (ii) The fusion protein relaxes supercoiled DNA, an activity that can be immunoprecipitated by anti-topoisomerase I serum. (iii) Sequence analysis has revealed that the longest cDNA clone (3645 base pairs) encodes a protein of 765 amino acids that shares 42% identity with Saccharomyces cerevisiae topoisomerase I. The sequence data also show that the catalytically active 67.7-kDa fragment is comprised of the carboxyl terminus. IS - 8 JF - Proceedings of the National Academy of Sciences of the United States of America AD - Department of Cell Biology and Anatomy, Johns Hopkins University School of Medicine, Baltimore, MD 21205. EP - 2547 TI - cDNA cloning of human DNA topoisomerase I: catalytic activity of a 67.7-kDa carboxyl-terminal fragment. VL - 85 SP - 2543 KW - coletta KW - gene KW - topoisomerase AU - D'Arpa, P AU - Machlin, PS AU - Ratrie, H AU - Rothfield, NF AU - Cleveland, DW AU - Earnshaw, WC PY - 1988/April// UR - http://view.ncbi.nlm.nih.gov/pubmed/2833744 ER -