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Proteomic insights into mannan degradation and protein secretion by the forest floor bacterium Chitinophaga pinensis

Larsbrink, Johan, 1982 (author)
KTH,Wallenberg Wood Science Center
Tuveng, T. R. (author)
Norges miljø- og biovitenskapelige universitet (NMBU),Norwegian University of Life Sciences (NMBU)
Pope, P. B. (author)
Norges miljø- og biovitenskapelige universitet (NMBU),Norwegian University of Life Sciences (NMBU)
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Bulone, Vincent (author)
Alba Nova Universitetscentrum,AlbaNova University Center. Stockholm Center for Physics, Astronomy and Biotechnology,University of Adelaide
Eijsink, V. (author)
Norges miljø- og biovitenskapelige universitet (NMBU),Norwegian University of Life Sciences (NMBU)
Brumer, Harry (author)
KTH,Wallenberg Wood Science Center
McKee, Lauren S., 1985- (author)
KTH,Glykovetenskap,Wallenberg Wood Science Center
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 (creator_code:org_t)
Elsevier BV, 2017
2017
English.
In: Journal of Proteomics. - : Elsevier BV. - 1874-3919 .- 1876-7737. ; 156, s. 63-74
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • Together with fungi, saprophytic bacteria are central to the decomposition and recycling of biomass in forest environments. The Bacteroidetes phylum is abundant in diverse habitats, and several species have been shown to be able to deconstruct a wide variety of complex carbohydrates. The genus Chid/lop/lap is often enriched in hotspots of plant and microbial biomass degradation. We present a proteomic assessment of the ability of Chitinophaga pinensis to grow on and degrade mannan polysaccharides, using an agarose plate-based method of protein collection to minimise contamination with exopolysaccharides and proteins from lysed cells, and to reflect the realistic setting of growth on a solid surface. We show that select Polysaccharide Utilisation Loci (PULs) are expressed in different growth conditions, and identify enzymes that may be involved in mannan degradation. By comparing proteomic and enzymatic profiles, we show evidence for the induced expression of enzymes and PULs in cells grown on mannan polysaccharides compared with cells grown on glucose. In addition, we show that the secretion of putative biomass-degrading enzymes during growth on glucose comprises a system for nutrient scavenging, which employs constitutively produced enzymes. Significance of this study: Chitinophaga pinensis belongs to a bacterial genus which is prominent in microbial communities in agricultural and forest environments, where plant and fungal biomass is intensively degraded. Such degradation is hugely significant in the recycling of carbon in the natural environment, and the enzymes responsible are of biotechnological relevance in emerging technologies involving the deconstruction of plant cell wall material. The bacterium has a comparatively large genome, which includes many uncharacterised carbohydrate -active enzymes. We present the first proteomic assessment of the biomass-degrading machinery of this species, focusing on mannan, an abundant plant cell wall hemicellulose. Our findings include the identification of several novel enzymes, which are promising targets for future biochemical characterisation. In addition, the data indicate the expression of specific Polysaccharide Utilisation Loci. induced in the presence of different growth substrates. We also highlight how a constitutive secretion of enzymes which deconstruct microbial biomass likely forms part of a nutrient scavenging process. (C) 2017 Elsevier B.V. All rights reseivecl.

Subject headings

LANTBRUKSVETENSKAPER  -- Lantbruksvetenskap, skogsbruk och fiske -- Skogsvetenskap (hsv//swe)
AGRICULTURAL SCIENCES  -- Agriculture, Forestry and Fisheries -- Forest Science (hsv//eng)
TEKNIK OCH TEKNOLOGIER  -- Miljöbioteknik (hsv//swe)
ENGINEERING AND TECHNOLOGY  -- Environmental Biotechnology (hsv//eng)
NATURVETENSKAP  -- Biologi -- Mikrobiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Microbiology (hsv//eng)

Keyword

Galactoglucomannan
cellvibrio-japonicus
Secretome
ller gl
substrate-specificity
Biochemistry & Molecular Biology
CAZyme
phanerochaete-chrysosporium
analytical chemistry
1959
hydrolase family
Label-free quantification
Chitinophaga pinensis
v31
p237
beta domain
gliding motility
cleary bv
system
konjac glucomannan
pa14 domain
v139
carbohydrate research
postia-placenta
1985
p426

Publication and Content Type

art (subject category)
ref (subject category)

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