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Tytuł pozycji:

Substrate Recognition of MARTX Ras/Rap1-Specific Endopeptidase.

Tytuł:
Substrate Recognition of MARTX Ras/Rap1-Specific Endopeptidase.
Autorzy:
Biancucci M; Department of Microbiology-Immunology, Northwestern University Feinberg School of Medicine , Chicago, Illinois 60611, United States.
Rabideau AE; Department of Chemistry, Massachusetts Institute of Technology , Cambridge, Massachusetts 02139, United States.
Lu Z; Department of Chemistry, Massachusetts Institute of Technology , Cambridge, Massachusetts 02139, United States.
Loftis AR; Department of Chemistry, Massachusetts Institute of Technology , Cambridge, Massachusetts 02139, United States.
Pentelute BL; Department of Chemistry, Massachusetts Institute of Technology , Cambridge, Massachusetts 02139, United States.
Satchell KJF; Department of Microbiology-Immunology, Northwestern University Feinberg School of Medicine , Chicago, Illinois 60611, United States.
Źródło:
Biochemistry [Biochemistry] 2017 May 30; Vol. 56 (21), pp. 2747-2757. Date of Electronic Publication: 2017 May 11.
Typ publikacji:
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
Język:
English
Imprint Name(s):
Original Publication: Washington, American Chemical Society.
MeSH Terms:
Bacterial Toxins/*chemistry
Bacterial Toxins/*metabolism
Endopeptidases/*chemistry
Endopeptidases/*metabolism
Vibrio vulnificus/*enzymology
rap1 GTP-Binding Proteins/*metabolism
ras Proteins/*metabolism
Humans ; Models, Molecular ; Substrate Specificity ; rap1 GTP-Binding Proteins/chemistry ; ras Proteins/chemistry
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Grant Information:
R01 AI092825 United States AI NIAID NIH HHS; T32 GM008334 United States GM NIGMS NIH HHS; R37 AI092825 United States AI NIAID NIH HHS; R01 AI051490 United States AI NIAID NIH HHS; R01 AI098369 United States AI NIAID NIH HHS
Substance Nomenclature:
0 (Bacterial Toxins)
EC 3.4.- (Endopeptidases)
EC 3.6.5.2 (rap1 GTP-Binding Proteins)
EC 3.6.5.2 (ras Proteins)
Entry Date(s):
Date Created: 20170502 Date Completed: 20170623 Latest Revision: 20220731
Update Code:
20240105
PubMed Central ID:
PMC5626579
DOI:
10.1021/acs.biochem.7b00246
PMID:
28459538
Czasopismo naukowe
Ras/Rap1-specific endopeptidase (RRSP) is a cytotoxic effector domain of the multifunctional autoprocessing repeats-in-toxin (MARTX) toxin of highly virulent strains of Vibrio vulnificus. RRSP blocks RAS-MAPK kinase signaling by cleaving Ras and Rap1 within the switch I region between Y32 and D33. Although the RRSP processing site is highly conserved among small GTPases, only Ras and Rap1 have been identified as proteolytic substrates. Here we report that residues Y32 and D33 at the scissile bond play an important role in RRSP substrate recognition, while the nucleotide state of Ras has an only minimal effect. In addition, substrate specificity is generated by residues across the entire switch I region. Indeed, swapping the Ras switch I region into either RalA or RhoA, GTPases that are not recognized by RRSP, generated chimeras that are substrates of RRSP. However, a difference in the processing efficiency of Ras switch I in the context of Ras, RalA, or RhoA indicates that protein regions outside Ras switch I also contribute to efficient RRSP substrate recognition. Moreover, we show that synthetic peptides corresponding to the Ras and Rap1, but not RalA, switch I regions are cleaved by RRSP, demonstrating sequence-specific substrate recognition. In conclusion, this work demonstrates that the GTPase recognition of RRSP is independent of the nucleotide state and is mainly driven by the Ras and Rap1 switch I loop and also influenced by additional protein-protein interactions, increasing the substrate specificity of RRSP.

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