ArticlePloS one2018
3-methylcrotonyl Coenzyme A (CoA) carboxylase complex is involved in the Xanthomonas citri subsp. citri lifestyle during citrus infection.
Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 13 citations in OpenAlex.
- Kog1 Represses Lipid Accumulation inJournal of fungi (Basel, Switzerland) · 2026Article
- Substrate-enhanced filamentation of 3-methylcrotonyl-CoA carboxylase inbioRxiv : the preprint server for biology · 2025Article
- Factors Affecting Non-Enzymatic Protein Acylation byMetabolites · 2024Article
- A computational model of Pseudomonas syringae metabolism unveils a role for branched-chain amino acids in Arabidopsis leaf colonization.PLoS computational biology · 2023Article
- Beauveria bassiana rewires molecular mechanisms related to growth and defense in tomato.Journal of experimental botany · 2023Article
- The Effects of Carbon Source and Growth Temperature on the Fatty Acid Profiles ofFrontiers in molecular biosciences · 2022Article
- Cinnamaldehyde inhibits the growth ofPeerJ · 2021Article
- trans-3-Methylglutaconyl CoA isomerization-dependent protein acylation.Biochemical and biophysical research communications · 2021Article
- A novel multidomain acyl-CoA carboxylase in Saccharopolyspora erythraea provides malonyl-CoA for de novo fatty acid biosynthesis.Scientific reports · 2019Article
- Herbicidal Activity and Molecular Docking Study of Novel ACCase Inhibitors.Frontiers in plant science · 2018Article
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Authors and funding
7 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Citrus canker is a disease caused by the phytopathogen Xanthomonas citri subsp. citri (Xcc), bacterium which is unable to survive out of the host for extended periods of time. Once established inside the plant, the pathogen must compete for resources and evade the defenses of the host cell. However, a number of aspects of Xcc metabolic and nutritional state, during the epiphytic stage and at different phases of infection, are poorly characterized. The 3-methylcrotonyl-CoA carboxylase complex (MCC) is an essential enzyme for the catabolism of the branched-chain amino acid leucine, which prevents the accumulation of toxic intermediaries, facilitates the generation of branched chain fatty acids and/or provides energy to the cell. The MCC complexes belong to a group of acyl-CoA carboxylases (ACCase) enzymes dependent of biotin. In this work, we have identified two ORFs (XAC0263 and XAC0264) encoding for the α and β subunits of an acyl-CoA carboxylase complex from Xanthomonas and demonstrated that this enzyme has MCC activity both in vitro and in vivo. We also found that this MCC complex is conserved in a group of pathogenic gram negative bacteria. The generation and analysis of an Xcc mutant strain deficient in MCC showed less canker lesions in the interaction with the host plant, suggesting that the expression of these proteins is necessary for Xcc fitness during infection.
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