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@ARTICLE{Yu:33246,
author = {Yu, T.-W. and Müller, R. and Müller, M. and Floss, H. G.},
title = {{M}utational analysis and reconstituted expression of the
biosynthetic genes involved in the formation of
3-amino-5-hydroxybenzoic acid : the starter unit of
rifamycin biosynthesis in {A}mycolatopsis mediterranei
{S}699},
journal = {The journal of biological chemistry},
volume = {276},
issn = {0021-9258},
address = {Bethesda, Md.},
publisher = {Soc.},
reportid = {PreJuSER-33246},
pages = {12546 - 12555},
year = {2001},
note = {Record converted from VDB: 12.11.2012},
abstract = {To investigate a novel branch of the shikimate biosynthesis
pathway operating in the formation of
3-amino-5-hydroxybenzoic acid (AHBA), the unique
biosynthetic precursor of rifamycin and related ansamycins,
a series of target-directed mutations and heterologous gene
expressions were investigated in Amycolatopsis mediterranei
and Streptomyces coelicolor. The genes involved in AHBA
formation were inactivated individually, and the resulting
mutants were further examined by incubating the cell-free
extracts with known intermediates of the pathway and
analyzing for AHBA formation. The rifL, -M, and -N genes
were shown to be involved in the step(s) from either
phosphoenolpyruvate/d-erythrose 4-phosphate or other
precursors to 3,4-dideoxy-4-amino-d-arabino-heptulosonate
7-phosphate. The gene products of the rifH, -G, and -J genes
resemble enzymes involved in the shikimate biosynthesis
pathway (August, P. R., Tang, L., Yoon, Y. J., Ning, S.,
Müller, R., Yu, T.-W., Taylor, M., Hoffmann, D., Kim,
C.-G., Zhang, X., Hutchinson, C. R., and Floss, H. G. (1998)
Chem. Biol. 5, 69-79). Mutants of the rifH and -J genes
produced rifamycin B at $1\%$ and $10\%,$ respectively, of
the yields of the wild type; inactivation of the rifG gene
did not affect rifamycin production significantly. Finally,
coexpressing the rifG-N and -J genes in S. coelicolor YU105
under the control of the act promoter led to significant
production of AHBA in the fermented cultures, confirming
that seven of these genes are indeed necessary and
sufficient for AHBA formation. The effects of deletion of
individual genes from the heterologous expression cassette
on AHBA formation duplicated the effects of the genomic
rifG-N and -J mutations on rifamycin production, indicating
that all these genes encode proteins with catalytic rather
than regulatory functions in AHBA formation for rifamycin
biosynthesis by A. mediterranei.},
keywords = {Actinomycetales: enzymology / Actinomycetales: genetics /
Amino Acid Sequence / Aminobenzoic Acids: metabolism / Base
Sequence / DNA Mutational Analysis: methods / DNA Primers /
Genes, Bacterial / Genes, Regulator / Molecular Sequence
Data / Multigene Family / Open Reading Frames / Plasmids /
Promoter Regions, Genetic / Restriction Mapping / Rifabutin:
metabolism / Rifamycins: biosynthesis / Aminobenzoic Acids
(NLM Chemicals) / DNA Primers (NLM Chemicals) / Rifamycins
(NLM Chemicals) / Rifabutin (NLM Chemicals) /
3-amino-5-hydroxybenzoic acid (NLM Chemicals) / J (WoSType)},
cin = {IBT-2},
ddc = {570},
cid = {I:(DE-Juel1)VDB56},
pnm = {Verfahrenstechnik zur mikrobiellen Gewinnung von
Primärmetaboliten},
pid = {G:(DE-Juel1)FUEK93},
shelfmark = {Biochemistry $\&$ Molecular Biology},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:11278540},
UT = {WOS:000168198600013},
doi = {10.1074/jbc.M009667200},
url = {https://juser.fz-juelich.de/record/33246},
}