Open AccessFunctional conservation between the argininosuccinate lyase of the archaeon Methanococcus maripaludis and the corresponding bacterial and eukaryal genes
Author(s) -
CohenKupiec R.,
Kupiec M.,
Sandbeck K.,
Leigh J.A.
Publication year - 1999
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1999.tb13507.x
Subject(s) - genetics , methanococcus , biology , gene , argininosuccinate lyase , escherichia coli , amino acid , arginine , urea cycle
The arg H gene encoding argininosuccinate lyase (ASL) of Methanococcus maripaludis was cloned on a 4.7‐kb H i n dIII genomic fragment. The gene is preceded by a short open reading frame (ORF149), which encodes a polypeptide with an unknown function. The two genes are co‐transcribed. The ASL of M. maripaludis shares a high amino acid identity with ASLs from both bacterial and eukaryal origins and was able to complement both an arg H Escherichia coli mutant and an arg4 yeast mutant, showing its extraordinary evolutionary conservation. Attempts to create an arg H auxotroph of M. maripaludis by disrupting the genomic allele were unsuccessful: although a knockout allele of arg H was integrated into the M. maripaludis chromosome by homologous recombination, the intact copy was not excluded, suggesting that the arg H gene is essential.