title: A propeptide-independent protease from Tannerella sp.6_1_58FAA_CT1 displays trypsin-like specificity.
abstract: Despite the absence of any homologs of Tannerella forsythia KLIKK proteases in Tannerella sp.6_1_58FAA_CT1, the strain possesses a putative cysteine protease (G9S4N1) closely related to RgpB of Porphyromonas gingivalis. G9S4N1 lacks obvious propeptide that behaves as inhibitor of proteases and was proven to be a propeptide-independent protease. Unlike RgpB, which exclusively cleaves ArgXaa bonds, G9S4N1 exhibits both arginine- and citrulline-specific activities. Mutations of Asp177, a potential P1-Arg binding site, to uncharged or positively charged residues did not alter the substrate specificity of G9S4N1 significantly. Moreover, a group of arginine-specific proteases from different species including porcine trypsin, bovine thrombin, and a trypsin-like serine protease of dengue 2 virus CF40-Gly-NS3pro185 also display different specificity toward citrulline residue, suggesting that citrulline-modified protein might have different roles and destiny in biological processes involving various proteases.
authors.affiliation: College of Pharmacy and Tianjin Key Laboratory of Molecular Drug Research, Nankai University, Tianjin, P. R. China.
authors.forename: Qitao
authors.initials: Q
authors.lastname: Song
authors.affiliation: College of Pharmacy and Tianjin Key Laboratory of Molecular Drug Research, Nankai University, Tianjin, P. R. China.
authors.forename: Xiaoyue
authors.initials: X
authors.lastname: Zhang
authors.affiliation: College of Pharmacy and Tianjin Key Laboratory of Molecular Drug Research, Nankai University, Tianjin, P. R. China.
authors.forename: Na
authors.initials: N
authors.lastname: Li
authors.affiliation: College of Pharmacy and Tianjin Key Laboratory of Molecular Drug Research, Nankai University, Tianjin, P. R. China.
authors.forename: Jie
authors.initials: J
authors.lastname: Shen
authors.affiliation: College of Pharmacy and Tianjin Key Laboratory of Molecular Drug Research, Nankai University, Tianjin, P. R. China.
authors.forename: Jiansong
authors.initials: J
authors.lastname: Cheng
mesh_terms: D018829:Adhesins, Bacterial / Q000235:genetics; D000818:Animals; D001120:Arginine / Q000378:metabolism; D041963:Bacteroidetes / Q000201:enzymology* / Q000378:metabolism; D001665:Binding Sites; D002417:Cattle; D002956:Citrulline / Q000235:genetics / Q000378:metabolism; D003546:Cysteine Endopeptidases / Q000235:genetics; D057056:Cysteine Proteases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000080867:Gingipain Cysteine Endopeptidases; D007700:Kinetics; D008239:Lysine / Q000378:metabolism; D008958:Models, Molecular; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity; D013552:Swine; D000070436:Tannerella forsythia; D014357:Trypsin / Q000378:metabolism
chemical_list: D018829:Adhesins, Bacterial; D000080867:Gingipain Cysteine Endopeptidases; D011994:Recombinant Proteins; D002956:Citrulline; D001120:Arginine; D057056:Cysteine Proteases; D014357:Trypsin; D003546:Cysteine Endopeptidases; D008239:Lysine
keywords: Citrulline; Propeptide; Protease; Tannerella; Trypsin-like