Novel stand-alone RAM domain protein-mediated catalytic control of anthranilate phosphoribosyltransferase in tryptophan biosynthesis in Thermus thermophilus.

Tetsuo Kubota, Hajime Matsushita, Takeo Tomita, Saori Kosono, Minoru Yoshida, Tomohisa Kuzuyama, Makoto Nishiyama

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Article in Extremophiles : life under extreme conditions, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

0.3field-weighted citation impact, top 30% of its field

1 · What the graph read from it

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3 · Its place in the literature

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1 citing paper in PubMed, 4 citations in OpenAlex.

International Conference on Extremophiles 2016.Extremophiles : life under extreme conditions · 2017
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4 · The record

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5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Tetsuo KubotaBiotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.

Hajime MatsushitaBiotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.

Takeo TomitaBiotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.

Saori KosonoBiotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.

Minoru YoshidaRIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wako, Saitama, 351-0198, Japan.

Tomohisa KuzuyamaBiotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.

Makoto NishiyamaBiotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan. umanis@mail.ecc.u-tokyo.ac.jp.

The University of Tokyo · JPRIKEN Center for Sustainable Resource Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Regulation of amino acid metabolism (RAM) domains are widely distributed among prokaryotes. In most cases, a RAM domain fuses with a DNA-binding domain to act as a transcriptional regulator. The extremely thermophilic bacterium, Thermus thermophilus, only carries a single gene encoding a RAM domain-containing protein on its genome. This protein is a stand-alone RAM domain protein (SraA) lacking a DNA-binding domain. Therefore, we hypothesized that SraA, which senses amino acids through its RAM domain, may interact with other proteins to modify its functions. In the present study, we identified anthranilate phosphoribosyltransferase (AnPRT), the second enzyme in the tryptophan biosynthetic pathway, as a partner protein that interacted with SraA in T. thermophilus. In the presence of tryptophan, SraA was assembled to a decamer and exhibited the ability to form a stable hetero-complex with AnPRT. An enzyme assay revealed that AnPRT was only inhibited by tryptophan in the presence of SraA. This result suggests a novel feedback control mechanism for tryptophan biosynthesis through an inter-RAM domain interaction in bacteria.

Indexed as

Anthranilate PhosphoribosyltransferaseBacterial ProteinsBinding SitesFeedback, PhysiologicalProtein BindingProtein MultimerizationThermus thermophilusTryptophanAnthranilate PhosphoribosyltransferaseBacterial ProteinsTryptophanAnthranilate phosphoribosyltransferaseFeedback inhibitionRAM domainThermus thermophilusTryptophan biosynthesis

Identifiers

PMID27757697

DOI10.1007/s00792-016-0884-0

OpenAlexW2535590975

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.