Heteroatom-participated lignin cleavage to functionalized aromatics

2020 ◽  
Vol 49 (12) ◽  
pp. 3748-3763 ◽  
Author(s):  
Hongji Li ◽  
Anon Bunrit ◽  
Ning Li ◽  
Feng Wang
Keyword(s):  

Heteroatom-containing reagents triggered the catalytic cleavage of lignin linkages and functionalization of products simultaneously.

Author(s):  
Changzhou Chen ◽  
Dichao Wu ◽  
Peng Liu ◽  
Haihong Xia ◽  
Minghao Zhou ◽  
...  

Noble-metal catalytic cleavage of the ether bonds in lignin to obtain aromatic chemicals had achieved great success, and development of a low-cost and efficient catalyst was crucial. Herein, NixLay/CNT was...


1992 ◽  
Vol 114 (5) ◽  
pp. 1903-1905 ◽  
Author(s):  
Janet R. Morrow ◽  
Lisa A. Buttrey ◽  
Valerie M. Shelton ◽  
Kristin A. Berback

2019 ◽  
Vol 47 (10) ◽  
pp. 1156-1163 ◽  
Author(s):  
Donglu Zhang ◽  
Aimee Fourie-O’Donohue ◽  
Peter S. Dragovich ◽  
Thomas H. Pillow ◽  
Jack D. Sadowsky ◽  
...  

2020 ◽  
Vol 117 (48) ◽  
pp. 30370-30379
Author(s):  
Wei Xie ◽  
Ivica Sowemimo ◽  
Rippei Hayashi ◽  
Juncheng Wang ◽  
Thomas R. Burkard ◽  
...  

Nibbler (Nbr) is a 3′-to-5′ exoribonuclease whose catalytic 3′-end trimming activity impacts microRNA (miRNA) and PIWI-interacting RNA (piRNA) biogenesis. Here, we report on structural and functional studies to decipher the contributions of Nbr’s N-terminal domain (NTD) and exonucleolytic domain (EXO) in miRNA 3′-end trimming. We have solved the crystal structures of the NTD core and EXO domains of Nbr, both in the apo-state. The NTD-core domain ofAedes aegyptiNbr adopts a HEAT-like repeat scaffold with basic patches constituting an RNA-binding surface exhibiting a preference for binding double-strand RNA (dsRNA) over single-strand RNA (ssRNA). Structure-guided functional assays inDrosophilaS2 cells confirmed a principal role of the NTD in exonucleolytic miRNA trimming, which depends on basic surface patches. Gain-of-function experiments revealed a potential role of the NTD in recruiting Nbr to Argonaute-bound small RNA substrates. The EXO domain ofA. aegyptiandDrosophila melanogasterNbr adopt a mixed α/β-scaffold with a deep pocket lined by a DEDDy catalytic cleavage motif. We demonstrate that Nbr’s EXO domain exhibits Mn2+-dependent ssRNA-specific 3′-to-5′ exoribonuclease activity. Modeling of a 3′ terminal Uridine into the catalytic pocket of Nbr EXO indicates that 2′-O-methylation of the 3′-U would result in a steric clash with a tryptophan side chain, suggesting that 2′-O-methylation protects small RNAs from Nbr-mediated trimming. Overall, our data establish that Nbr requires its NTD as a substrate recruitment platform to execute exonucleolytic miRNA maturation, catalyzed by the ribonuclease EXO domain.


1955 ◽  
Vol 77 (2) ◽  
pp. 501-501 ◽  
Author(s):  
Francis Binkley
Keyword(s):  

ChemInform ◽  
2010 ◽  
Vol 25 (9) ◽  
pp. no-no
Author(s):  
P. KUMAR ◽  
V. R. HEGDE ◽  
B. PANDEY ◽  
T. RAVINDRANATHAN

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