A structural model for (GlcNAc)2 translocation via a periplasmic chitooligosaccharide-binding protein from marine Vibrio bacteria

Kitaoku, Yoshihito; Fukamizo, Tamo; Kumsaoad, Sawitree; Ubonbal, P.; Robinson, Robert; Suginta, Wipa

doi:10.1016/j.jbc.2021.101071

Cited by 3 publications

(3 citation statements)

References 47 publications

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Section: Resultsmentioning

confidence: 96%

“…Specifically, Kitaoku et. al ., reported on a chitoporin specific to chitin found in Vibrio spp (31). Homologues can also be found in other proteomes, such as E. coli and A. veronii .…”

Section: Resultsmentioning

confidence: 99%

“…In fact, we found abundant GH20s in the cellular proteomics experiments of both strains (A. rivuli WP_042039723 and A. bestiarum A0A291U507, SI EXCEL DOC 1). Different mechanism have been reported which transport monomers and dimers through the inner cell membrane (Figure 4) (9,14,31,32). First, chitin is cleaved into GlcNAc oligomers by several endochitinases (GH18_1 GH18_2 and GH19), followed by terminal cleavage through exo-chitinase (GH20).…”

Section: Chitin Degradation and Utilization Routes In A Rivuli And A ...mentioning

confidence: 99%

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Exploring the metabolic potential ofAeromonasto utilise the carbohydrate polymer chitin

Tugui,

Sorokin,

Hijnen

et al. 2024

Preprint

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Members of the Aeromonas genus are commonly found in natural aquatic ecosystems. However, they are also frequently present in non-chlorinated drinking water distribution systems. High densities of these bacteria indicate favorable conditions for microbial regrowth, which is considered undesirable. Studies have indicated that the presence of Aeromonas is associated with loose deposits and the presence of invertebrates, specifically Asellus aquaticus. Therefore, a potential source of nutrients in these nutrient poor environments is chitin, the structural shell component in these invertebrates. In this study, we demonstrate the ability of two Aeromonas strains, commonly encountered in drinking water distribution systems, to effectively degrade and utilize chitin as a sole carbon and nitrogen source. We conducted a quantitative proteomics study on the cell biomass and secretome of both strains, revealing a dedicated and diverse spectrum of hydrolytic enzymes and pathways for the uptake and metabolism of chitin. Furthermore, when the primary nutrient source was switched from glucose to chitin, more than half of the Aeromonas proteome showed significant changes. Additionally, a genomic analysis of Aeromonas species found in drinking water distribution systems suggests a general potential ability of this genus to degrade and utilize a variety of carbohydrate biopolymers. This study indicates the relation between the utilization of chitin by Aeromonas and their association with invertebrates such as A. aquaticus in loose deposits in drinking water distribution systems. This knowledge provides the foundation for the development of more effective water sanitation strategies.

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Section: Resultsmentioning

confidence: 96%

“…Specifically, Kitaoku et. al ., reported on a chitoporin specific to chitin found in Vibrio spp (31). Homologues can also be found in other proteomes, such as E. coli and A. veronii .…”

Section: Resultsmentioning

confidence: 99%

Section: Chitin Degradation and Utilization Routes In A Rivuli And A ...mentioning

confidence: 99%

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Exploring the metabolic potential ofAeromonasto utilise the carbohydrate polymer chitin

Tugui,

Sorokin,

Hijnen

et al. 2024

Preprint

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Periplasmic chitooligosaccharide-binding protein requires a three-domain organization for substrate translocation

Ohnuma,

Tsujii,

Kataoka

et al. 2023

Sci Rep

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Periplasmic solute-binding proteins (SBPs) specific for chitooligosaccharides, (GlcNAc)n (n = 2, 3, 4, 5 and 6), are involved in the uptake of chitinous nutrients and the negative control of chitin signal transduction in Vibrios. Most translocation processes by SBPs across the inner membrane have been explained thus far by two-domain open/closed mechanism. Here we propose three-domain mechanism of the (GlcNAc)n translocation based on experiments using a recombinant VcCBP, SBP specific for (GlcNAc)n from Vibrio cholerae. X-ray crystal structures of unliganded or (GlcNAc)3-liganded VcCBP solved at 1.2–1.6 Å revealed three distinct domains, the Upper1, Upper2 and Lower domains for this protein. Molecular dynamics simulation indicated that the motions of the three domains are independent and that in the (GlcNAc)3-liganded state the Upper2/Lower interface fluctuated more intensively, compared to the Upper1/Lower interface. The Upper1/Lower interface bound two GlcNAc residues tightly, while the Upper2/Lower interface appeared to loosen and release the bound sugar molecule. The three-domain mechanism proposed here was fully supported by binding data obtained by thermal unfolding experiments and ITC, and may be applicable to other translocation systems involving SBPs belonging to the same cluster.

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Exploring the metabolic potential of Aeromonas to utilise the carbohydrate polymer chitin

Tugui,

Sorokin,

Hijnen

et al. 2025

RSC Chem. Biol.

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A structural model for (GlcNAc)2 translocation via a periplasmic chitooligosaccharide-binding protein from marine Vibrio bacteria

Cited by 3 publications

References 47 publications

Exploring the metabolic potential ofAeromonasto utilise the carbohydrate polymer chitin

Exploring the metabolic potential ofAeromonasto utilise the carbohydrate polymer chitin

Periplasmic chitooligosaccharide-binding protein requires a three-domain organization for substrate translocation

Exploring the metabolic potential of Aeromonas to utilise the carbohydrate polymer chitin

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