The structural basis for high-affinity uptake of lignin-derived aromatic compounds by proteobacterial TRAP transporters.
Bacterial Proteins
/ genetics
Biodegradation, Environmental
Biological Transport
/ genetics
Gene Expression Regulation, Bacterial
/ genetics
Ligands
Lignin
/ chemistry
Membrane Transport Proteins
/ chemistry
Oxidoreductases
/ genetics
Periplasm
/ genetics
Periplasmic Binding Proteins
/ genetics
Proteobacteria
/ genetics
RNA-Binding Proteins
/ genetics
Rhodopseudomonas
/ genetics
Transcription Factors
/ genetics
Chromohalobacter salexigens
Rhodopseudomonas palustris
Sagittula stellata
hydroxycinnamate
tripartite ATP-independent periplasmic transporter
Journal
The FEBS journal
ISSN: 1742-4658
Titre abrégé: FEBS J
Pays: England
ID NLM: 101229646
Informations de publication
Date de publication:
01 2022
01 2022
Historique:
revised:
13
07
2021
received:
22
04
2021
accepted:
09
08
2021
pubmed:
11
8
2021
medline:
19
2
2022
entrez:
10
8
2021
Statut:
ppublish
Résumé
The organic polymer lignin is a component of plant cell walls, which like (hemi)-cellulose is highly abundant in nature and relatively resistant to degradation. However, extracellular enzymes released by natural microbial consortia can cleave the β-aryl ether linkages in lignin, releasing monoaromatic phenylpropanoids that can be further catabolised by diverse species of bacteria. Biodegradation of lignin is therefore important in global carbon cycling, and its natural abundance also makes it an attractive biotechnological feedstock for the industrial production of commodity chemicals. Whilst the pathways for degradation of lignin-derived aromatics have been extensively characterised, much less is understood about how they are recognised and taken up from the environment. The purple phototrophic bacterium Rhodopseudomonas palustris can grow on a range of phenylpropanoid monomers and is a model organism for studying their uptake and breakdown. R. palustris encodes a tripartite ATP-independent periplasmic (TRAP) transporter (TarPQM) linked to genes encoding phenylpropanoid-degrading enzymes. The periplasmic solute-binding protein component of this transporter, TarP, has previously been shown to bind aromatic substrates. Here, we determine the high-resolution crystal structure of TarP from R. palustris as well as the structures of homologous proteins from the salt marsh bacterium Sagittula stellata and the halophile Chromohalobacter salexigens, which also grow on lignin-derived aromatics. In combination with tryptophan fluorescence ligand-binding assays, our ligand-bound co-crystal structures reveal the molecular basis for high-affinity recognition of phenylpropanoids by these TRAP transporters, which have potential for improving uptake of these compounds for biotechnological transformations of lignin.
Substances chimiques
Bacterial Proteins
0
Ligands
0
Membrane Transport Proteins
0
MtrB protein, Bacteria
0
Periplasmic Binding Proteins
0
RNA-Binding Proteins
0
Transcription Factors
0
Lignin
9005-53-2
Oxidoreductases
EC 1.-
aryl ether cleaving enzyme
EC 1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
436-456Subventions
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/F016832/1
Pays : United Kingdom
Informations de copyright
© 2021 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
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