Methyl group transfer upon gas phase decomposition of protonated methyl benzoate and similar compounds

2018 ◽  
Vol 53 (5) ◽  
pp. 379-384 ◽  
Author(s):  
Rafał Frański ◽  
Błażej Gierczyk ◽  
Maciej Zalas ◽  
Wojciech Jankowski ◽  
Marcin Hoffmann
Keyword(s):  
Gas Phase ◽  
Methyl Benzoate ◽  
Phase Decomposition ◽  
Methyl Group ◽  
Group Transfer ◽  
Methyl Group Transfer

scholarly journals Novel insights into the m6A-RNA methyltransferase METTL3 in cancer

2021 ◽  
Vol 9 (1) ◽  
Author(s):  
Yiqing Cai ◽  
Rui Feng ◽  
Tiange Lu ◽  
Xiaomin Chen ◽  
Xiangxiang Zhou ◽  
...  
Keyword(s):  
Poor Prognosis ◽  
Human Cancer ◽  
Rna Modification ◽  
Rapid Progression ◽  
Antitumor Therapy ◽  
Promoting Effect ◽  
Methyl Group ◽  
Group Transfer ◽  
Functional Regulation ◽  
Methyl Group Transfer

AbstractN6-methyladenosine (m6A) is a prevalent internal RNA modification in higher eukaryotic cells. As the pivotal m6A regulator, RNA methyltransferase-like 3 (METTL3) is responsible for methyl group transfer in the progression of m6A modification. This epigenetic regulation contributes to the structure and functional regulation of RNA and further promotes tumorigenesis and tumor progression. Accumulating evidence has illustrated the pivotal roles of METTL3 in a variety of human cancers. Here, we systemically summarize the interaction between METTL3 and RNAs, and illustrate the multiple functions of METTL3 in human cancer. METLL3 is aberrantly expressed in a variety of tumors. Elevation of METTL3 is usually associated with rapid progression and poor prognosis of tumors. On the other hand, METTL3 may also function as a tumor suppressor in several cancers. Based on the tumor-promoting effect of METTL3, the possibility of applying METTL3 inhibitors is further discussed, which is expected to provide novel insights into antitumor therapy.

scholarly journals Proteogenomics Reveals Novel Reductive Dehalogenases and Methyltransferases Expressed during Anaerobic Dichloromethane Metabolism

2019 ◽  
Vol 85 (6) ◽  
Author(s):  
Sara Kleindienst ◽  
Karuna Chourey ◽  
Gao Chen ◽  
Robert W. Murdoch ◽  
Steven A. Higgins ◽  
...  
Keyword(s):  
Amino Acid ◽  
Reductive Dechlorination ◽  
Bond Cleavage ◽  
Amino Acid Identity ◽  
Methyl Group ◽  
Acid Identity ◽  
Group Transfer ◽  
Degrading Bacterium ◽  
Chlorine Bond ◽  
Methyl Group Transfer

ABSTRACTDichloromethane (DCM) is susceptible to microbial degradation under anoxic conditions and is metabolized via the Wood-Ljungdahl pathway; however, mechanistic understanding of carbon-chlorine bond cleavage is lacking. The microbial consortium RM contains the DCM degrader “CandidatusDichloromethanomonas elyunquensis” strain RM, which strictly requires DCM as a growth substrate. Proteomic workflows applied to DCM-grown consortium RM biomass revealed a total of 1,705 nonredundant proteins, 521 of which could be assigned to strain RM. In the presence of DCM, strain RM expressed a complete set of Wood-Ljungdahl pathway enzymes, as well as proteins implicated in chemotaxis, motility, sporulation, and vitamin/cofactor synthesis. Four corrinoid-dependent methyltransferases were among the most abundant proteins. Notably, two of three putative reductive dehalogenases (RDases) encoded within strain RM’s genome were also detected in high abundance. Expressed RDase 1 and RDase 2 shared 30% amino acid identity, and RDase 1 was most similar to an RDase ofDehalococcoides mccartyistrain WBC-2 (AOV99960, 52% amino acid identity), while RDase 2 was most similar to an RDase ofDehalobactersp. strain UNSWDHB (EQB22800, 72% amino acid identity). Although the involvement of RDases in anaerobic DCM metabolism has yet to be experimentally verified, the proteome characterization results implicated the possible participation of one or more reductive dechlorination steps and methyl group transfer reactions, leading to a revised proposal for an anaerobic DCM degradation pathway.IMPORTANCENaturally produced and anthropogenically released DCM can reside in anoxic environments, yet little is known about the diversity of organisms, enzymes, and mechanisms involved in carbon-chlorine bond cleavage in the absence of oxygen. A proteogenomic approach identified two RDases and four corrinoid-dependent methyltransferases expressed by the DCM degrader “CandidatusDichloromethanomonas elyunquensis” strain RM, suggesting that reductive dechlorination and methyl group transfer play roles in anaerobic DCM degradation. These findings suggest that the characterized DCM-degrading bacteriumDehalobacterium formicoaceticumand “CandidatusDichloromethanomonas elyunquensis” strain RM utilize distinct strategies for carbon-chlorine bond cleavage, indicating that multiple pathways evolved for anaerobic DCM metabolism. The specific proteins (e.g., RDases and methyltransferases) identified in strain RM may have value as biomarkers for monitoring anaerobic DCM degradation in natural and contaminated environments.

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