Characterization of a Novel Subtilisin-like Protease Myroicolsin from Deep Sea Bacterium Myroides profundi D25 and Molecular Insight into Its Collagenolytic Mechanism

Ran, Ling; Su, Hai-Nan; Zhou, Mingyang; Wang, Lei; Chen, Xiu-Lan; Xie, Bin-Bin; Song, Xin; Qin, Qi‐Long; Pang, Xiuhua; Zhou, Biao; Zhang, Yuzhong; Zhang, Xiying

doi:10.1074/jbc.m113.513861

Cited by 35 publications

(52 citation statements)

References 56 publications

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“…SM9913 (Zhao et al, 2008; Ran et al, 2013), the thermostable protease from Geobacillus collagenovorans MO-1 (Okamoto et al, 2001), AcpII from Alkalimonas collagenimarina AC40 (Kurata et al, 2010), and myroicolsin from Myroides profundi D25 (Ran et al, 2014). P57 has collagenolytic activity and its PA domain has collagen-binding ability, indicating that P57 is an S8 serine collagenolytic protease.…”

Section: Discussionmentioning

confidence: 99%

“…It has been found that protease-producing bacteria and their extracellular proteases are rich and diverse in marine sediments (Olivera et al, 2007; Zhou et al, 2009, 2013). Some proteases from marine sedimentary bacteria have been characterized, most of which are shown to have special properties, such as cold adaptation (Chen et al, 2007; Yan et al, 2009; Kurata et al, 2010; Yang et al, 2013), salt tolerance (Yan et al, 2009), distinct substrate specificity and catalytic mechanism (Ran et al, 2014). Therefore, marine sediments are good resources for exploring novel proteases.…”

Section: Introductionmentioning

confidence: 99%

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Characterization of a New S8 serine Protease from Marine Sedimentary Photobacterium sp. A5–7 and the Function of Its Protease-Associated Domain

Li¹,

Tang

Shao

et al. 2016

Front. Microbiol.

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Bacterial extracellular proteases are important for bacterial nutrition and marine sedimentary organic nitrogen degradation. However, only a few proteases from marine sedimentary bacteria have been characterized. Some subtilases have a protease-associated (PA) domain inserted in the catalytic domain. Although structural analysis and deletion mutation suggests that the PA domain in subtilases is involved in substrate binding, direct evidence to support this function is still absent. Here, a protease, P57, secreted by Photobacterium sp. A5-7 isolated from marine sediment was characterized. P57 could hydrolyze casein, gelatin and collagen. It showed the highest activity at 40°C and pH 8.0. P57 is a new subtilase, with 63% sequence identity to the closest characterized protease. Mature P57 contains a catalytic domain and an inserted PA domain. The recombinant PA domain from P57 was shown to have collagen-binding ability, and Phe349 and Tyr432 were revealed to be key residues for collagen binding in the PA domain. This study first shows direct evidence that the PA domain of a subtilase can bind substrate, which provides a better understanding of the function of the PA domain of subtilases and bacterial extracellular proteases from marine sediment.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Characterization of a New S8 serine Protease from Marine Sedimentary Photobacterium sp. A5–7 and the Function of Its Protease-Associated Domain

Li¹,

Tang

Shao

et al. 2016

Front. Microbiol.

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“…Thus, myroicolsin gains access to the attack sites on collagen monomers. Finally, the fibrillar structure of collagen is completely destroyed, and collagen monomers are degraded into peptides and free amino acids (66).…”

Section: Bacterial Serine Collagenolytic Proteases From the S8 Familymentioning

confidence: 99%

Diversity, Structures, and Collagen-Degrading Mechanisms of Bacterial Collagenolytic Proteases

Zhang¹,

Ran²,

Li³

et al. 2015

Appl Environ Microbiol

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113

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Bacterial collagenolytic proteases are important because of their essential role in global collagen degradation and because of their virulence in some human bacterial infections. Bacterial collagenolytic proteases include some metalloproteases of the M9 family from Clostridium or Vibrio strains, some serine proteases distributed in the S1, S8, and S53 families, and members of the U32 family. In recent years, there has been remarkable progress in discovering new bacterial collagenolytic proteases and in investigating the collagen-degrading mechanisms of bacterial collagenolytic proteases. This review provides comprehensive insight into bacterial collagenolytic proteases, especially focusing on the structures and collagen-degrading mechanisms of representative bacterial collagenolytic proteases in each family. The roles of bacterial collagenolytic proteases in human diseases and global nitrogen cycling, together with the biotechnological and medical applications for these proteases, are also briefly discussed.

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“…Chitin and collagens are important sources of nutrients and energy in the marine environment, and their degradation by various microorganisms contributes to global carbon and nitrogen cycling (8)(9)(10)(11)(12). In V. cholerae, the chitin utilization program is a well-characterized, hierarchical process that involves bacterial chemotaxis toward the substrate, binding of the bacteria to abiotic or biotic chitinous surfaces mediated by several proteins, including GbpA, and finally the degradation of chitin, which is accomplished by extracellular chitinases ChiA-1 and ChiA-2, periplasmic hydrolases specific for chitin oligosaccharides as well as cytoplasmic enzymes (8,(13)(14)(15).…”

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confidence: 99%

A Metalloprotease Secreted by the Type II Secretion System Links Vibrio cholerae with Collagen

et al. 2015

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bVibrio cholerae is autochthonous to various aquatic niches and is the etiological agent of the life-threatening diarrheal disease cholera. The persistence of V. cholerae in natural habitats is a crucial factor in the epidemiology of cholera. In contrast to the well-studied V. cholerae-chitin connection, scarce information is available about the factors employed by the bacteria for the interaction with collagens. Collagens might serve as biologically relevant substrates, because they are the most abundant protein constituents of metazoan tissues and V. cholerae has been identified in association with invertebrate and vertebrate marine animals, as well as in a benthic zone of the ocean where organic matter, including collagens, accumulates. Here, we describe the characterization of the V. cholerae putative collagenase, VchC, encoded by open reading frame VC1650 and belonging to the subfamily M9A peptidases. Our studies demonstrate that VchC is an extracellular collagenase degrading native type I collagen of fish and mammalian origin. Alteration of the predicted catalytic residues coordinating zinc ions completely abolished the protein enzymatic activity but did not affect the translocation of the protease by the type II secretion pathway into the extracellular milieu. We also show that the protease undergoes a maturation process with the aid of a secreted factor(s). Finally, we propose that V. cholerae is a collagenovorous bacterium, as it is able to utilize collagen as a sole nutrient source. This study initiates new lines of investigations aiming to uncover the structural and functional components of the V. cholerae collagen utilization program. Members of the genus Vibrio are important inhabitants of the marine coastal waters, estuaries, and ocean sediments, with some pathogenic species also causing wound infections, primary septicemia, gastroenteritis, and diarrhea in humans (1, 2). Among the more than 200 serogroups of V. cholerae, only O1 and O139 are recognized as agents of cholera, a potentially life-threatening diarrheal disease. Cholera remains a significant public health problem by affecting millions of people annually, predominantly in developing countries that have limited clean water supplies and poor sanitation (3). Infection of the human host occurs upon ingestion of water or food contaminated with the bacterium. Following colonization of the small intestine, V. cholerae utilizes a multicomponent secretory pathway, the type II secretion system (T2SS), to release cholera toxin. Cholera toxin induces acute diarrhea in people infected with cholera, enabling the bacteria to escape from the host into the aquatic reservoir (4). During interepidemic periods, V. cholerae persists freely or in association with various aquatic organisms, including copepods, insect egg masses, shellfish, and vertebrate fish (5-7). Extracellular proteins, including those secreted by the T2SS, have been implicated in facilitating the fitness of V. cholerae in both the human host and aquatic niches (4,6,8). The array of extrace...

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Characterization of a Novel Subtilisin-like Protease Myroicolsin from Deep Sea Bacterium Myroides profundi D25 and Molecular Insight into Its Collagenolytic Mechanism

Cited by 35 publications

References 56 publications

Characterization of a New S8 serine Protease from Marine Sedimentary Photobacterium sp. A5–7 and the Function of Its Protease-Associated Domain

Characterization of a New S8 serine Protease from Marine Sedimentary Photobacterium sp. A5–7 and the Function of Its Protease-Associated Domain

Diversity, Structures, and Collagen-Degrading Mechanisms of Bacterial Collagenolytic Proteases

A Metalloprotease Secreted by the Type II Secretion System Links Vibrio cholerae with Collagen

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