Non-enzymatic action of expansins

Cosgrove, Daniel J.

doi:10.1074/jbc.l120.013410

Cited by 7 publications

(3 citation statements)

References 4 publications

(2 reference statements)

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“…EcMltA utilizes only one acidic amino acid to cleave the β-1,4-glycosidic bonds in bacterial cell wall peptidoglycan ( 36 ). Nevertheless, the apparent lack of lytic activity for PcaLOOLs is in line with extensive experimental evidence debunking the proposed lytic action of expansins ( 37 ).…”

Section: Resultssupporting

confidence: 67%

Loosenin-Like Proteins from Phanerochaete carnosa Impact Both Cellulose and Chitin Fiber Networks

Monschein

Ioannou

Koitto

et al. 2023

Appl Environ Microbiol

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The present study deepens investigations of microbial expansin-related proteins and their applied significance by (i) reporting a detailed comparison of diverse loosenins encoded by the same organism, (ii) considering both cellulosic and chitin-containing materials as targeted substrates, and (iii) investigating the impact of the C-terminal carbohydrate binding module (CBM) present in other expansin-related proteins on loosenin function. By revealing the potential of fungal loosenins to impact both cellulose and chitin-containing networks, our study reveals a possible biological and applied role of loosenins in fungal cell wall processing.

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Section: Resultssupporting

confidence: 67%

Loosenin-Like Proteins from Phanerochaete carnosa Impact Both Cellulose and Chitin Fiber Networks

Monschein

Ioannou

Koitto

et al. 2023

Appl Environ Microbiol

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“…EcMltA utilizes only one acidic amino acid to cleave the β-1,4-glycosidic bonds in bacterial cell wall peptidoglycan (51). Nevertheless, the apparent lack of lytic activity for PcaLOOLs is in line with extensive experimental evidence debunking the proposed lytic action of expansins (52).…”

Section: Resultssupporting

confidence: 67%

Loosenin-like proteins fromPhanerochaete carnosaimpact both cellulose and chitin fiber networks

Monschein¹,

Ioannou²,

Amin³

et al. 2022

Preprint

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Microbial expansin-related proteins are ubiquitous across bacterial and fungal organisms, and reportedly play a role in the modification and deconstruction of cell wall polysaccharides including lignocellulose. So far, very few microbial expansin related proteins, including loosenins and loosenin-like (LOOL) proteins, have been functionally characterized. Herein, four LOOLs encoded by Phanerochaete carnosa and belonging to different subfamilies (i.e., PcaLOOL7 and PcaLOOL9 from subfamily A; PcaLOOL2 and PcaLOOL12 from subfamily B) were recombinantly produced and the purified proteins were characterized using diverse cellulose and chitin substrates. Whereas all of the purified PcaLOOLs weakened cellulose filter paper and cellulose nanofibril networks (CNF), none significantly boosted cellulase activity on the selected cellulose substrates (Avicel and Whatman paper). Binding of PcaLOOLs to alpha-chitin was higher than to cellulose (Avicel), and highest at pH 5.0. Notably, whereas PcaLOOL9 reduced the yield strain of chitin nanofibrils (ChNF) in a protein-dose dependent manner, the reverse pattern was observed for PcaLOOL7 despite belonging to the same LOOL subfamily. The current study reveals the potential of microbial expansin-related proteins to impact both cellulose and chitin networks, and provides further evidence pointing to a non-lytic mode of action.

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“…The authors declare that they have no conflicts of interest with the contents of this article. 1 To whom correspondence may be addressed. E-mail: gregg.beckham@ nrel.gov.…”

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confidence: 99%