TY - JOUR
T1 - Cysteine biosynthesis in the Archaea
T2 - Methanosarcina thermophila utilizes O-acetylserine sulfhydrylase
AU - Borup, Birthe
AU - Ferry, James G.
N1 - Funding Information:
This work was funded by NASA Ames Cooperative Agreement NCC21059 and DOE Grant DE-FG02-95ER20198. We thank Jennifer Loveland-Curtze for help with cell lyophilization, Robert J. Durso for donating the S. cerevisiae strain and helping with culturing and making cell extract. We also thank Birgit Alber for the M. thermophila DNA, Robert Barber for the plasmid DNA library, and Jonna Coombs, Peter P. Sheridan and Robert Barber for critical reading of the manuscript.
PY - 2000/8/15
Y1 - 2000/8/15
N2 - Two pathways for cysteine biosynthesis are known in nature; however, it is not known which, if either, the Archaea utilize. Enzyme activities in extracts of Methanosarcina thermophila grown with combinations of cysteine and sulfide as sulfur sources indicated that this archaeon utilizes the pathway found in the Bacteria domain. The genes encoding serine transacetylase and O-acetylserine sulfhydrylase (cysE and cysK) are adjacent on the chromosome of M. thermophila and possibly form an operon. When M. thermophila is grown with cysteine as the sole sulfur source, O-acetylserine sulfhydrylase activity is maximally expressed suggesting alternative roles for this enzyme apart from cysteine biosynthesis. (C) 2000 Federation of European Microbiological Societies.
AB - Two pathways for cysteine biosynthesis are known in nature; however, it is not known which, if either, the Archaea utilize. Enzyme activities in extracts of Methanosarcina thermophila grown with combinations of cysteine and sulfide as sulfur sources indicated that this archaeon utilizes the pathway found in the Bacteria domain. The genes encoding serine transacetylase and O-acetylserine sulfhydrylase (cysE and cysK) are adjacent on the chromosome of M. thermophila and possibly form an operon. When M. thermophila is grown with cysteine as the sole sulfur source, O-acetylserine sulfhydrylase activity is maximally expressed suggesting alternative roles for this enzyme apart from cysteine biosynthesis. (C) 2000 Federation of European Microbiological Societies.
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U2 - 10.1016/S0378-1097(00)00284-6
DO - 10.1016/S0378-1097(00)00284-6
M3 - Article
C2 - 10930739
AN - SCOPUS:0034663994
SN - 0378-1097
VL - 189
SP - 205
EP - 210
JO - FEMS Microbiology Letters
JF - FEMS Microbiology Letters
IS - 2
ER -