Journal of Microbiology

Journal Article

FgIlv3a is crucial in branched-chain amino acid biosynthesis, vegetative differentiation, and virulence in Fusarium graminearum: Xin Liu , Yichen Jiang , Yinghui Zhang , Mingzheng Yu , Hongjun Jiang , Jianhong Xu , Jianrong Shi; J. Microbiol. 2019;57(8):694-703. Published online May 11, 2019; DOI: https://doi.org/10.1007/s12275-019-9123-6

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Dihydroxyacid dehydratase (DHAD), encoded by ILV3, catalyses the third step in the biosynthetic pathway of branchedchain amino acids (BCAAs), which include isoleucine (Ile), leucine (Leu), and valine (Val). Enzymes involved in BCAA biosynthesis exist in bacteria, plants, and fungi but not in mammals and are therefore attractive targets for antimicrobial or herbicide development. In this study, three paralogous ILV3 genes (FgILV3A, FgILV3B, and FgILV3C) were identified in the genome of Fusarium graminearum, the causal agent of Fusarium head blight (FHB). Deletion of FgILV3A alone or combined with FgILV3B or FgILV3C indicated an important role for FgILV3A in BCAA biosynthesis. FgILV3A deletion mutants lost the ability to grow on medium lacking amino acids. Exogenous supplementation of 1 mM Ile and Val rescued the auxotrophy of ΔFgIlv3A, though 5 mM was required to recover the growth defects in ΔFgIlv3AB and ΔFgIlv3AC strains, indicating that FgIlv3b and FgIlv3c exhibit redundant but accessory roles with FgIlv3a in BCAA biosynthesis. The auxotrophy of ΔFgIlv3A resulted in pleiotropic defects in aerial hyphal growth, in conidial formation and germination, and in aurofusarin accumulation. In addition, the mutants showed reduced virulence and deoxynivalenol production. Overall, our study demonstrates that FgIlv3a is crucial for BCAA biosynthesis in F. graminearum and a candidate fungicide target for FHB management.

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Gary Jones, Jane Usher, Joel T. Steyer, Richard B. Todd
Essays in Biochemistry.2023; 67(5): 865. CrossRef
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Research Support, Non-U.S. Gov't

X-ray Structure of Prephenate Dehydratase from Streptococcus mutans: Min Hyung Shin , Hyung-Keun Ku , Jin Sue Song , Saehae Choi , Se Young Son , Hee-Dai Kim , Sook-Kyung Kim , Il Yeong Park , Soo Jae Lee; J. Microbiol. 2014;52(6):490-495. Published online March 7, 2014; DOI: https://doi.org/10.1007/s12275-014-3645-8

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Abstract

Prephenate dehydratase is a key enzyme of the biosynthesis of L-phenylalanine in the organisms that utilize shikimate pathway. Since this enzymatic pathway does not exist in mammals, prephenate dehydratase can provide a new drug targets for antibiotics or herbicide. Prephenate dehydratase is an allosteric enzyme regulated by its end product. The enzyme composed of two domains, catalytic PDT domain located near the N-terminal and regulatory ACT domain located near the C-terminal. The allosteric enzyme is suggested to have two different conformations. When the regulatory molecule, phenylalanine, is not bound to its ACT domain, the catalytic site of PDT domain maintain open (active) state conformation as Sa-PDT structure. And the open state of its catalytic site become closed (allosterically inhibited) state if the regulatory molecule is bound to its ACT domain as Ct-PDT structure. However, the X-ray structure of prephenate dehydratase from Streptococcus mutans (Sm-PDT) shows that the catalytic site of Sm-PDT has closed state conformation without phenylalanine molecule bound to its regulatory site. The structure suggests a possibility that the binding of phenylalanine in its regulatory site may not be the only prerequisite for the closed state conformation of Sm-PDT.

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Computational investigations of allostery in aromatic amino acid biosynthetic enzymes
Wanting Jiao
Biochemical Society Transactions.2021; 49(1): 415. CrossRef
Feedback inhibition of the prephenate dehydratase from Saccharomyces cerevisiae and its mutation in huangjiu (Chinese rice wine) yeast
Shuangping Liu, Qilin Yang, Jieqi Mao, Mei Bai, Jiandi Zhou, Xiao Han, Jian Mao
LWT.2020; 133: 110040. CrossRef

Journal Article

Alternative Production of Avermectin Components in Streptomyces avermitilis by Gene Replacement: Joon-Hyoung Yong , Woo-Hyeon Byeon; J. Microbiol. 2005;43(3):277-284.; DOI: https://doi.org/2212 [pii]

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Abstract: The avermectins are composed of eight compounds, which exhibit structural differences at three positions. A family of four closely-related major components, A1a, A2a, B1a and B2a, has been identified. Of these components, B1a exhibits the most potent antihelminthic activity. The coexistence of the "1" components and "2" components has been accounted for by the defective dehydratase of aveAI module 2, which appears to be responsible for C22-23 dehydration. Therefore, we have attempted to replace the dehydratase of aveAI module 2 with the functional dehydratase from the erythromycin eryAII module 4, via homologous recombination. Erythromycin polyketide synthetase should contain the sole dehydratase domain, thus generating a saturated chain at the C6-7 of erythromycin. We constructed replacement plasmids with PCR products, by using primers which had been derived from the sequences of avermectin aveAI and the erythromycin eryAII biosynthetic gene cluster. If the original dehydratase of Streptomyces avermitilis were exchanged with the corresponding erythromycin gene located on the replacement plasmid, it would be expected to result in the formation of precursors which contain alkene at C22-23, formed by the dehydratase of erythromycin module 4, and further processed by avermectin polyketide synthase. Consequently, the resulting recombinant strain JW3105, which harbors the dehydratase gene derived from erythromycin, was shown to produce only C22,23-unsaturated avermectin compounds. Our research indicates that the desired compound may be produced via polyketide gene replacement.

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