Genetics of the serine cycle in Methylobacterium extorquens AM1: identification, sequence, and mutation of three new genes involved in C1 assimilation, orf4, mtkA, and mtkB.
نویسندگان
چکیده
In a recent paper we reported the sequence of the beginning of a serine cycle gene cluster on the Methylobacterium extorquens AM1 chromosome, containing the genes encoding serine glyoxylate aminotransferase (sgaA), hydroxypyruvate reductase (hprA), and 5,10-methylenetetrahydrofolate dehydrogenase (mtdA) (L. V. Chistoserdova and M. E. Lidstrom J. Bacteriol. 176:1957-1968, 1994). Here we present the sequence of the adjacent downstream region containing three full and one partial open reading frames. The first of the full open reading frames (orf4) remains unidentified, while the other two (mtkA and mtkB) code for the two subunits of malate thiokinase, and the fourth, a partial open reading frame (ppcA), apparently encodes phosphoenolpyruvate carboxylase. Mutants containing insertion mutations in orf4, mtdA, and mtdB all were unable to grow on C1 compounds, showing that these three newly identified genes are indispensable for the operation of the serine cycle. Mutants in orf4 were also unable to grow on C2 compounds, but growth was restored by glyoxylate, suggesting that orf4 might be required for the conversion of acetyl coenzyme A to glyoxylate.
منابع مشابه
QscR, a LysR-type transcriptional regulator and CbbR homolog, is involved in regulation of the serine cycle genes in Methylobacterium extorquens AM1.
A new gene, qscR, encoding a LysR-type transcriptional regulator that is a homolog of CbbR, has been characterized from the facultative methylotroph Methylobacterium extorquens AM1 and shown to be the major regulator of the serine cycle, the specific C1 assimilation pathway. The qscR mutant was shown to be unable to grow on C1 compounds, and it lacked the activity of serine-glyoxylate aminotran...
متن کاملGenetics of the serine cycle in Methylobacterium extorquens AM1: cloning, sequence, mutation, and physiological effect of glyA, the gene for serine hydroxymethyltransferase.
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....
متن کاملQscR-mediated transcriptional activation of serine cycle genes in Methylobacterium extorquens AM1.
QscR, a LysR-type regulator, is the major regulator of assimilatory C1 metabolism in Methylobacterium extorquens AM1. It has been shown to interact with the promoters of the two operons that encode the majority of the serine cycle enzymes (sga-hpr-mtdA-fch for the qsc1 operon and mtkA-mtkB-ppc-mclA for the qsc2 operon), as well as with the promoter of glyA and its own promoter. To obtain furthe...
متن کاملGenetics of the serine cycle in Methylobacterium extorquens AM1: identification of sgaA and mtdA and sequences of sgaA, hprA, and mtdA.
In a previous paper, we reported identification of the 5' part of hprA of Methylobacterium extorquens AM1, which encodes the serine cycle enzyme hydroxypyruvate reductase (L. V. Chistoserdova and M. E. Lidstrom, J. Bacteriol. 174:71-77, 1992). Here we present the complete sequence of hprA and partial sequence of genes adjacent to hprA. Upstream of hprA, the 3' part of an open reading frame was ...
متن کاملIdentification and mutation of a gene required for glycerate kinase activity from a facultative methylotroph, Methylobacterium extorquens AM1.
A gene (gckA) responsible for the activity of glycerate kinase has been identified within a chromosomal fragment of the serine cycle methylotroph Methylobacterium extorquens AM1. A mutation in gckA leads to a specific C1-negative phenotype. The polypeptide sequence derived from gckA showed high similarity to a product of ttuD essential for tartrate metabolism in Agrobacterium vitis. Our data su...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Journal of bacteriology
دوره 176 23 شماره
صفحات -
تاریخ انتشار 1994