Proteomics

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In vivo characterization of the bacterial intramembrane-cleaving protease RseP using the heme binding tag-based assay iCliPSpy

ABSTRACT: Purified, putative unprocessed and processed MBPmut-TNFa fusion proteins were analyzed by LC-MS. The average molecular weights of the eluted MBPmut-TNFa fusion proteins obtained by deconvolution of the ESI-MS spectra are given. For MBPmut-TNFa preparations from “Empty vector control” and “RseP-Myc H22F”, we found a protein eluting at 9.1 with an average molecular weight of about 45448 Da min, which was higher than expected for a MBPmut-TNFa fusion protein and was therefore not further characterized. Compounds eluting at retention times above 9.5 min (corresponding to 90 % acetonitrile) were contaminants not further characterized. a to e belong to one experiment, and the processing specificity of RseP wt was confirmed in this experiment by analysis of RsePMyc wt. The C-terminal sequences of the substrate MBPmut- … CPFLSLFSFL39 fusion protein and processing product MBPmut- … CPFLSLF36 were confirmed by LC-MS/MS analysis.

INSTRUMENT(S): impact II

ORGANISM(S): Escherichia Coli

SUBMITTER: Rabea Goetz  

LAB HEAD: Carsten Hopf

PROVIDER: PXD038785 | Pride | 2023-03-20

REPOSITORIES: Pride

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In vivo characterization of the bacterial intramembrane-cleaving protease RseP using the heme binding tag-based assay iCliPSpy.

Kupke Thomas T   Götz Rabea M RM   Richter Florian M FM   Beck Rainer R   Lolicato Fabio F   Nickel Walter W   Hopf Carsten C   Brügger Britta B  

Communications biology 20230318 1

Regulated intramembrane proteolysis (RIP) describes the protease-dependent cleavage of transmembrane proteins within the hydrophobic core of cellular membranes. Intramembrane-cleaving proteases (I-CliPs) that catalyze these reactions are found in all kingdoms of life and are involved in a wide range of cellular processes, including signaling and protein homeostasis. I-CLiPs are multispanning membrane proteins and represent challenging targets in structural and enzyme biology. Here we introduce i  ...[more]

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