Purine biosynthesis in Escherichia coli K12: structure and DNA sequence studies of the purHD locus.

Abstract:

:The de novo purine biosynthetic enzymes 5-amino-4-imidazolecarboxamide-ribonucleotide (AICAR) transformylase (EC 2.1.2.3), IMP cyclohydrolase (EC 3.5.4.10) and glycineamide-ribonucleotide (GAR) synthetase (EC 2.1.2.2) are encoded by the purHD locus of Escherichia coli. The DNA sequence of this locus revealed two open reading frames encoding polypeptides of Mr 57,335 and 45,945 (GAR synthetase), respectively, that formed an operon. The DNA sequence, maxicell and complementation analyses all supported the concept that the Mr 57,335 polypeptide is the product of the purH gene and encodes a bifunctional protein containing both AICAR transformylase and IMP cyclohydrolase activities. The 5' end of the purHD mRNA was determined by primer extension mapping and contains two regions of dyad symmetry capable of forming 'hairpin' loops where the formation of the one would prevent the formation of the other but not vice versa. Regulation by the purR gene product was explained by the discovery of a purR binding site in the purHD control region.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Flannigan KA,Hennigan SH,Vogelbacker HH,Gots JS,Smith JM

doi

10.1111/j.1365-2958.1990.tb00605.x

subject

Has Abstract

pub_date

1990-03-01 00:00:00

pages

381-92

issue

3

eissn

0950-382X

issn

1365-2958

journal_volume

4

pub_type

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