Evidence for Pentapeptide-Dependent and Independent CheB Methylesterases

Autor: Tino Krell, Félix Velando, Jose A. Gavira, Miguel A. Matilla, Miriam Rico-Jiménez
Přispěvatelé: European Commission, Ministerio de Ciencia, Innovación y Universidades (España), Ministerio de Economía y Competitividad (España)
Jazyk: angličtina
Rok vydání: 2020
Předmět:
0301 basic medicine
Chemoreceptor
chemoreceptor
Pectobacterium
medicine.disease_cause
Pentapeptide repeat
lcsh:Chemistry
Methylesterase
lcsh:QH301-705.5
Spectroscopy
chemistry.chemical_classification
methylesterase
biology
Chemotaxis
Salmonella enterica
General Medicine
Chemoreceptor Cells
Computer Science Applications
Chemosensory pathways
Biochemistry
Pseudomonas aeruginosa
Bacterial signal transduction
CheB
C-terminal pentapeptide
Signal Transduction
030106 microbiology
Article
Catalysis
Inorganic Chemistry
03 medical and health sciences
Bacterial Proteins
Escherichia coli
medicine
Amino Acid Sequence
Physical and Theoretical Chemistry
Molecular Biology
Pectobacterium atrosepticum
bacterial signal transduction
Binding Sites
Chemoreceptors
Organic Chemistry
Methyltransferases
biology.organism_classification
chemosensory pathways
030104 developmental biology
Enzyme
chemistry
lcsh:Biology (General)
lcsh:QD1-999
X-ray structure
Peptides
Carboxylic Ester Hydrolases
Bacteria
Zdroj: International Journal of Molecular Sciences, Vol 21, Iss 8459, p 8459 (2020)
International Journal of Molecular Sciences
Volume 21
Issue 22
Digital.CSIC. Repositorio Institucional del CSIC
instname
ISSN: 1661-6596
1422-0067
Popis: Many bacteria possess multiple chemosensory pathways that are composed of homologous signaling proteins. These pathways appear to be functionally insulated from each other, but little information is available on the corresponding molecular basis. We report here a novel mechanism that contributes to pathway insulation. We show that, of the four CheB paralogs of Pseudomonas aeruginosa PAO1, only CheB2 recognizes a pentapeptide at the C-terminal extension of the McpB (Aer2) chemoreceptor (KD = 93 µM). McpB is the sole chemoreceptor that stimulates the Che2 pathway, and CheB2 is the methylesterase of this pathway. Pectobacterium atrosepticum SCRI1043 has a single CheB, CheB_Pec, and 19 of its 36 chemoreceptors contain a C-terminal pentapeptide. The deletion of cheB_Pec abolished chemotaxis, but, surprisingly, none of the pentapeptides bound to CheB_Pec. To determine the corresponding structural basis, we solved the 3D structure of CheB_Pec. Its structure aligned well with that of the pentapeptide-dependent enzyme from Salmonella enterica. However, no electron density was observed in the CheB_Pec region corresponding to the pentapeptide-binding site in the Escherichia coli CheB. We hypothesize that this structural disorder is associated with the failure to bind pentapeptides. Combined data show that CheB methylesterases can be divided into pentapeptide-dependent and independent enzymes.
This research was funded by FEDER funds and the Fondo Social Europeo through grants from the Spanish Ministry for Science, Innovation and Universities to MAM (PID2019-103972GA-I00) and the Spanish Ministry of Economy and Competitiveness to JAG (BIO2016-74875-P) and TK (BIO2016-76779-P).
Databáze: OpenAIRE
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