Comparative Biochemical and Structural Analysis of Novel Cellulose Binding Proteins ($ T\overline{a}pirins\ $) from Extremely Thermophilic <em>Caldicellulosiruptor</em> Species [electronic resource]

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Tác giả:

Ngôn ngữ: eng

Ký hiệu phân loại: 547.7 Macromolecules and related compounds

Thông tin xuất bản: Washington, D.C. : Oak Ridge, Tenn. : United States. Dept. of Energy. Office of Science ; Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy, 2019

Mô tả vật lý: Size: Article No. e01983-18 : , digital, PDF file.

Bộ sưu tập: Metadata

ID: 262880

 Genomes of extremely thermophilic <
 em>
 Caldicellulosiruptor<
 /em>
  species encode novel cellulose binding proteins, called $ t\overline{a}pirins\ $, located proximate to the type IV pilus locus. The C-terminal domain of <
 named-content content-type='genus-species'>
 Caldicellulosiruptor kronotskyensis<
 /named-content>
  $ t\overline{a}pirin\ $ 0844 (Calkro_0844) is structurally unique and has a cellulose binding affinity akin to that seen with family 3 carbohydrate binding modules (CBM3s). Here, full-length and C-terminal versions of $ t\overline{a}pirins\ $ from <
 named-content content-type='genus-species'>
 Caldicellulosiruptor bescii<
 /named-content>
  (Athe_1870), <
 named-content content-type='genus-species'>
 Caldicellulosiruptor hydrothermalis<
 /named-content>
 (Calhy_0908), <
 named-content content-type='genus-species'>
 Caldicellulosiruptor kristjanssonii<
 /named-content>
  (Calkr_0826), and <
 named-content content-type='genus-species'>
 Caldicellulosiruptor naganoensis<
 /named-content>
  (NA10_0869) were produced recombinantly in <
 named-content content-type='genus-species'>
 Escherichia coli<
 /named-content>
  and compared to Calkro_0844. All five $ t\overline{a}pirins\ $ bound to microcrystalline cellulose, switchgrass, poplar, and filter paper but not to xylan. Densitometry analysis of bound protein fractions visualized by SDS-PAGE revealed that Calhy_0908 and Calkr_0826 (from weakly cellulolytic species) associated with the cellulose substrates to a greater extent than Athe_1870, Calkro_0844, and NA10_0869 (from strongly cellulolytic species). Perhaps this relates to their specific needs to capture glucans released from lignocellulose by cellulases produced in <
 em>
 Caldicellulosiruptor<
 /em>
  communities. Calkro_0844 and NA10_0869 share a higher degree of amino acid sequence identity (>
 80% identity) with each other than either does with Athe_1870 (~50%). The levels of amino acid sequence identity of Calhy_0908 and Calkr_0826 to Calkro_0844 were only 16% and 36%, respectively, although the three-dimensional structures of their C-terminal binding regions were closely related. Unlike the parent strain, <
 named-content content-type='genus-species'>
 C. bescii<
 /named-content>
  mutants lacking the $ t\overline{a}pirin\ $ genes did not bind to cellulose following short-term incubation, suggesting a role in cell association with plant biomass. Given the scarcity of carbohydrates in neutral terrestrial hot springs, $ t\overline{a}pirins\ $ likely help scavenge carbohydrates from lignocellulose to support growth and survival of <
 em>
 Caldicellulosiruptor<
 /em>
  species.The mechanisms by which microorganisms attach to and degrade lignocellulose are important to understand if effective approaches for conversion of plant biomass into fuels and chemicals are to be developed. <
 em>
 Caldicellulosiruptor<
 /em>
  species grow on carbohydrates from lignocellulose at elevated temperatures and have biotechnological significance for that reason. Novel cellulose binding proteins, called $ t\overline{a}pirins\ $, are involved in the way that <
 em>
 Caldicellulosiruptor<
 /em>
  species interact with microcrystalline cellulose, and additional information about the diversity of these proteins across the genus, including binding affinity and three-dimensional structural comparisons, is provided here.
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