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Molecular mechanism of environmental d-xylose perception by a XylFII-LytS complex in bacteria.

Li J, Wang C, Yang G, Sun Z, Guo H, Shao K, Gu Y, Jiang W, Zhang P
Proc Natl Acad Sci U S A 114 8235-8240 (2017)
Related entries: 5xsj, 5xss

Cited: 16 times
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Abstract

d-xylose, the main building block of plant biomass, is a pentose sugar that can be used by bacteria as a carbon source for bio-based fuel and chemical production through fermentation. In bacteria, the first step for d-xylose metabolism is signal perception at the membrane. We previously identified a three-component system in Firmicutes bacteria comprising a membrane-associated sensor protein (XylFII), a transmembrane histidine kinase (LytS) for periplasmic d-xylose sensing, and a cytoplasmic response regulator (YesN) that activates the transcription of the target ABC transporter xylFGH genes to promote the uptake of d-xylose. The molecular mechanism underlying signal perception and integration of these processes remains elusive, however. Here we purified the N-terminal periplasmic domain of LytS (LytSN) in a complex with XylFII and determined the conformational structures of the complex in its d-xylose-free and d-xylose-bound forms. LytSN contains a four-helix bundle, and XylFII contains two Rossmann fold-like globular domains with a xylose-binding cleft between them. In the absence of d-xylose, LytSN and XylFII formed a heterodimer. Specific binding of d-xylose to the cleft of XylFII induced a large conformational change that closed the cleft and brought the globular domains closer together. This conformational change led to the formation of an active XylFII-LytSN heterotetramer. Mutations at the d-xylose binding site and the heterotetramer interface diminished heterotetramer formation and impaired the d-xylose-sensing function of XylFII-LytS. Based on these data, we propose a working model of XylFII-LytS that provides a molecular basis for d-xylose utilization and metabolic modification in bacteria.

Articles - 5xsd mentioned but not cited (1)

  1. Molecular mechanism of environmental d-xylose perception by a XylFII-LytS complex in bacteria. Li J, Wang C, Yang G, Sun Z, Guo H, Shao K, Gu Y, Jiang W, Zhang P. Proc Natl Acad Sci U S A 114 8235-8240 (2017)


Reviews citing this publication (3)

  1. The role of solute binding proteins in signal transduction. Matilla MA, Ortega Á, Krell T. Comput Struct Biotechnol J 19 1786-1805 (2021)
  2. Functional Annotation of Bacterial Signal Transduction Systems: Progress and Challenges. Martín-Mora D, Fernández M, Velando F, Ortega Á, Gavira JA, Matilla MA, Krell T. Int J Mol Sci 19 E3755 (2018)
  3. Consolidated bioprocessing for butanol production of cellulolytic Clostridia: development and optimization. Wen Z, Li Q, Liu J, Jin M, Yang S. Microb Biotechnol 13 410-422 (2020)

Articles citing this publication (12)

  1. The Molecular Mechanism of Nitrate Chemotaxis via Direct Ligand Binding to the PilJ Domain of McpN. Martín-Mora D, Ortega Á, Matilla MA, Martínez-Rodríguez S, Gavira JA, Krell T. mBio 10 e02334-18 (2019)
  2. Discovery of an ene-reductase for initiating flavone and flavonol catabolism in gut bacteria. Yang G, Hong S, Yang P, Sun Y, Wang Y, Zhang P, Jiang W, Gu Y. Nat Commun 12 790 (2021)
  3. Determination of Ligand Profiles for Pseudomonas aeruginosa Solute Binding Proteins. Fernández M, Rico-Jiménez M, Ortega Á, Daddaoua A, García García AI, Martín-Mora D, Torres NM, Tajuelo A, Matilla MA, Krell T. Int J Mol Sci 20 E5156 (2019)
  4. Investigating Nutrient Limitation Role on Improvement of Growth and Poly(3-Hydroxybutyrate) Accumulation by Burkholderia sacchari LMG 19450 From Xylose as the Sole Carbon Source. Oliveira-Filho ER, Silva JGP, de Macedo MA, Taciro MK, Gomez JGC, Silva LF. Front Bioeng Biotechnol 7 416 (2019)
  5. Interface switch mediates signal transmission in a two-component system. Wang M, Guo Q, Zhu K, Fang B, Yang Y, Teng M, Li X, Tao Y. Proc Natl Acad Sci U S A 117 30433-30440 (2020)
  6. The Repertoire of Solute-Binding Proteins of Model Bacteria Reveals Large Differences in Number, Type, and Ligand Range. Ortega Á, Matilla MA, Krell T. Microbiol Spectr 10 e0205422 (2022)
  7. β-D-XYLOSIDASE 4 modulates systemic immune signaling in Arabidopsis thaliana. Bauer K, Nayem S, Lehmann M, Wenig M, Shu LJ, Ranf S, Geigenberger P, Vlot AC. Front Plant Sci 13 1096800 (2022)
  8. Characteristics of the GlnH and GlnX Signal Transduction Proteins Controlling PknG-Mediated Phosphorylation of OdhI and 2-Oxoglutarate Dehydrogenase Activity in Corynebacterium glutamicum. Sundermeyer L, Bosco G, Gujar S, Brocker M, Baumgart M, Willbold D, Weiergräber OH, Bellinzoni M, Bott M. Microbiol Spectr 10 e0267722 (2022)
  9. Deciphering Cellodextrin and Glucose Uptake in Clostridium thermocellum. Yan F, Dong S, Liu YJ, Yao X, Chen C, Xiao Y, Bayer EA, Shoham Y, You C, Cui Q, Feng Y. mBio 13 e0147622 (2022)
  10. Role of the Solute-Binding Protein CuaD in the Signaling and Regulating Pathway of Cellobiose and Cellulose Utilization in Ruminiclostridium cellulolyticum. Fosses A, Franche N, Parsiegla G, Denis Y, Maté M, de Philip P, Fierobe HP, Perret S. Microorganisms 11 1732 (2023)
  11. Structural basis of phosphorylation-induced activation of the response regulator VbrR. Hong S, Guo J, Zhang X, Zhou X, Zhang P, Yu F. Acta Biochim Biophys Sin (Shanghai) 55 43-50 (2023)
  12. The structure of B-ARR reveals the molecular basis of transcriptional activation by cytokinin. Zhou CM, Li JX, Zhang TQ, Xu ZG, Ma ML, Zhang P, Wang JW. Proc Natl Acad Sci U S A 121 e2319335121 (2024)


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