Rare variants of the FMN riboswitch class in Clostridium difficile and other bacteria exhibit altered ligand specificity.

Rare variants of the FMN riboswitch class in Clostridium difficile and other bacteria exhibit altered ligand specificity.
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DOI:
10.1261/rna.067975.118
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发表时间:
2019-01
期刊:
RNA (New York, N.Y.)
影响因子:
--
通讯作者:
Breaker RR
Breaker RR
中科院分区:
其他
文献类型:
--
作者:
Atilho RM;Perkins KR;Breaker RR

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许多细菌使用黄素单核苷酸(FMN)核糖开关来控制负责这种酶辅因子或其前体核黄素的生物合成和运输的基因的表达。在艰难梭菌和一些其他细菌的菌株中发现的FMN核糖开关的罕见变体通常控制注释为转运蛋白的蛋白质的表达,包括多药外排泵。这些RNA不再识别FMN,并且在通常参与辅助因子的核糖基和磷酸部分的结合的核苷酸位置处不同于原始核糖开关共有序列。发现两种变体亚型之一的代表结合FMN前体核黄素和FMN降解产物光黄素和光色素。虽然这些变异FMN核糖开关所感应的生物学相关配体仍不确定,但我们的研究结果表明,许多C。difficile可能使用罕见的核糖开关来感知黄素降解产物并激活转运蛋白以进行解毒。
Many bacteria use flavin mononucleotide (FMN) riboswitches to control the expression of genes responsible for the biosynthesis and transport of this enzyme cofactor or its precursor, riboflavin. Rare variants of FMN riboswitches found in strains of Clostridium difficile and some other bacteria typically control the expression of proteins annotated as transporters, including multidrug efflux pumps. These RNAs no longer recognize FMN, and differ from the original riboswitch consensus sequence at nucleotide positions normally involved in binding of the ribityl and phosphate moieties of the cofactor. Representatives of one of the two variant subtypes were found to bind the FMN precursor riboflavin and the FMN degradation products lumiflavin and lumichrome. Although the biologically relevant ligand sensed by these variant FMN riboswitches remains uncertain, our findings suggest that many strains of C. difficile might use rare riboswitches to sense flavin degradation products and activate transporters for their detoxification.
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