Genetics of the serine cycle in Methylobacterium extorquens AM1: cloning, sequence, mutation, and physiological effect of glyA, the gene for serine hydroxymethyltransferase. Export

@article{citeulike:2231722, abstract = {The gene (glyA) of Methylobacterium extorquens AM1 encoding serine hydroxymethyltransferase (SHMT), one of the key enzymes of the serine cycle for C1 assimilation, was isolated by using a synthetic oligonucleotide with a sequence based on amino acid sequence conserved in SHMTs from different sources. The amino acid sequence deduced from the gene revealed high similarity to those of known SHMTs. The cloned gene was inactivated by insertion of a kanamycin resistance gene, and recombination of this insertion derivative with the wild-type gene produced an SHMT null mutant. Surprisingly, this mutant had lost its ability to grow on C1 as well as on C2 compounds but was still able to grow on succinate. The DNA fragment containing glyA was shown not to be linked with fragments carrying serine cycle genes identified earlier, making it the fourth chromosomal region of M. extorquens AM1 to be indicated as being involved in C1 assimilation.}, author = {Chistoserdova, L. V. and Lidstrom, M. E.}, citeulike-article-id = {2231722}, citeulike-linkout-0 = {http://jb.asm.org/cgi/content/abstract/176/21/6759}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/7961431}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=7961431}, day = {1}, journal = {J. Bacteriol.}, keywords = {am1, am1\_enzymes}, month = {November}, number = {21}, pages = {6759--6762}, posted-at = {2008-01-14 19:44:18}, priority = {0}, title = {Genetics of the serine cycle in Methylobacterium extorquens AM1: cloning, sequence, mutation, and physiological effect of glyA, the gene for serine hydroxymethyltransferase.}, url = {http://jb.asm.org/cgi/content/abstract/176/21/6759}, volume = {176}, year = {1994} }

TY - JOUR ID - citeulike:2231722 L3 - citeulike-article-id:2231722 N2 - The gene (glyA) of Methylobacterium extorquens AM1 encoding serine hydroxymethyltransferase (SHMT), one of the key enzymes of the serine cycle for C1 assimilation, was isolated by using a synthetic oligonucleotide with a sequence based on amino acid sequence conserved in SHMTs from different sources. The amino acid sequence deduced from the gene revealed high similarity to those of known SHMTs. The cloned gene was inactivated by insertion of a kanamycin resistance gene, and recombination of this insertion derivative with the wild-type gene produced an SHMT null mutant. Surprisingly, this mutant had lost its ability to grow on C1 as well as on C2 compounds but was still able to grow on succinate. The DNA fragment containing glyA was shown not to be linked with fragments carrying serine cycle genes identified earlier, making it the fourth chromosomal region of M. extorquens AM1 to be indicated as being involved in C1 assimilation. IS - 21 JF - J. Bacteriol. EP - 6762 TI - Genetics of the serine cycle in Methylobacterium extorquens AM1: cloning, sequence, mutation, and physiological effect of glyA, the gene for serine hydroxymethyltransferase. VL - 176 SP - 6759 KW - am1 KW - am1_enzymes AU - Chistoserdova, LV AU - Lidstrom, ME PY - 1994/11/01/ UR - http://jb.asm.org/cgi/content/abstract/176/21/6759 ER -