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Putative methylomirabilis lanthanidiphila surface layer protein

ABSTRACT: Gambelli et al., 2021, investigate methylomirabilis bacteria, which perform anaerobic methane oxidation coupled to nitrite reduction via an intra-aerobic pathway to produce carbon dioxide and dinitrogen gas. These bacteria possess an unusual polygonal cell shape with sharp ridges that run along the cell body. Previously, a putative surface protein layer (S-layer) was observed as the outermost cell layer of these bacteria which has been further investigated in this study. Corresponding author Laura van Niftrik, Department of Microbiology, Faculty of Science, Radboud University, Nijmegen, 6525 AJ, the Netherlands.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Candidatus Methylomirabilis Sp. Lanth

SUBMITTER: Martin Pabst

LAB HEAD: Dr. Martin Pabst

PROVIDER: PXD029319 | Pride | 2022-01-06

REPOSITORIES: Pride

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			Action	DRS
	MP_16072020_LvN_S_layer_gps_5_DDA01.mgf	Mgf
	MP_16072020_LvN_S_layer_gps_5_DDA01.mzXML	Mzxml
	MP_16072020_LvN_S_layer_gps_5_DDA01.raw	Raw
	MP_CDR19082020_LvN_S_Layer_Chymotrypsin_DDA01.mgf	Mgf
	MP_CDR19082020_LvN_S_Layer_Chymotrypsin_DDA01.mzXML	Mzxml

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Project description:Gram-negative bacteria possess stress responses to maintain the integrity of the cell envelope. Stress sensors monitor outer membrane permeability, envelope protein folding, and energization of the inner membrane. The systems used by Gram-negative bacteria to sense and combat stress resulting from disruption of the peptidoglycan layer are not well characterized. The peptidoglycan layer is a single molecule that completely surrounds the cell and ensures its structural integrity. During cell growth new peptidoglcyan subunits are incorporated into the peptidoglycan layer by a series of enzymes called the penicillin-binding proteins (PBPs). To explore how Gram-negative bacteria respond to peptidoglycan stress, global gene expression analysis was used to identify Escherichia coli stress responses activated following inhibition of specific PBPs by the Î²-lactam antibiotics mecillinam and cefsulodin. Inhibition of PBPs with different roles in peptidoglycan synthesis has different consequences for cell morphology and viability, suggesting that not all perturbations to the peptidoglycan layer generate equivalent stresses. We demonstrate that inhibition of different PBPs resulted in both shared and unique stress responses. The regulation of capsular synthesis (Rcs) phosphorelay was activated by inhibition of all of the PBPs tested. Furthermore, we show that activation of the Rcs phosphorelay increased survival in the presence of these antibiotics, independently of capsule synthesis. Both activation of the phosphorelay and survival required signal transduction via the outer membrane lipoprotein RcsF and the response regulator RcsB. We propose that the Rcs pathway responds to peptidoglycan damage and contributes to the intrinsic resistance of E. coli to Î²-lactam antibiotics. We used microarrays to identify changes in gene expression resulting from treatment of Escherichia coli with the Î²-lactam antibiotics cefsulodin, mecillinam, or the combination. This SuperSeries is composed of the following subset Series:; GSE10158: Expression of Escherichia coli treated with cefsulodin and mecillinam, alone and in combination; GSE10159: Expression of Escherichia coli treated with cefsulodin and mecillinam, alone at the minimum inhibitory concentration Experiment Overall Design: Refer to individual Series

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Putative methylomirabilis lanthanidiphila surface layer protein

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