Secretion of genetically-engineered dihydrofolate reductase from Escherichia coli using an E. coli alpha-hemolysin membrane translocation system. Export

@article{citeulike:4387965, abstract = {Secretion of fusion proteins composed of cytoplasmic protein dihydrofolate reductase (DHFR) and the Escherichia coli alpha-haemolysin (HlyA) C-terminal sequence was examined through the haemolysin secretion machinery of E. coli. DHFR of various lengths was combined with the HlyA C-terminal region, and both secretion and DHFR activity of the fusions were measured. The secretion was found to be inversely correlated with the intracellular DHFR activity. Moreover, when one amino acid (Ile155) in a beta-sheet of the DHFR C-terminal region was replaced with Lys, the enzymatically active DHFR fusion protein was secreted into the medium. We discuss the possibility of a relationship between folding and secretion of HlyA-fused protein in the HlyA secretion system.}, author = {Nakano, H. and Kawakami, Y. and Nishimura, H.}, citeulike-article-id = {4387965}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/1368920}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=1368920}, issn = {0175-7598}, journal = {Applied microbiology and biotechnology}, keywords = {4grant, dhfr, hemolysin, hlyb, mtx, type-i}, month = {September}, number = {6}, pages = {765--771}, posted-at = {2009-04-23 17:07:45}, priority = {2}, title = {Secretion of genetically-engineered dihydrofolate reductase from Escherichia coli using an E. coli alpha-hemolysin membrane translocation system.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/1368920}, volume = {37}, year = {1992} }

TY - JOUR ID - citeulike:4387965 L3 - citeulike-article-id:4387965 N2 - Secretion of fusion proteins composed of cytoplasmic protein dihydrofolate reductase (DHFR) and the Escherichia coli alpha-haemolysin (HlyA) C-terminal sequence was examined through the haemolysin secretion machinery of E. coli. DHFR of various lengths was combined with the HlyA C-terminal region, and both secretion and DHFR activity of the fusions were measured. The secretion was found to be inversely correlated with the intracellular DHFR activity. Moreover, when one amino acid (Ile155) in a beta-sheet of the DHFR C-terminal region was replaced with Lys, the enzymatically active DHFR fusion protein was secreted into the medium. We discuss the possibility of a relationship between folding and secretion of HlyA-fused protein in the HlyA secretion system. IS - 6 JF - Applied microbiology and biotechnology SN - 0175-7598 EP - 771 TI - Secretion of genetically-engineered dihydrofolate reductase from Escherichia coli using an E. coli alpha-hemolysin membrane translocation system. VL - 37 SP - 765 KW - 4grant KW - dhfr KW - hemolysin KW - hlyb KW - mtx KW - type-i AU - Nakano, H AU - Kawakami, Y AU - Nishimura, H PY - 1992/09// UR - http://view.ncbi.nlm.nih.gov/pubmed/1368920 ER -