MRM2

更新于：2025-05-07

基本信息

别名

16S rRNA (uridine(1369)-2'-O)-methyltransferase、16S rRNA [Um1369] 2'-O-methyltransferase、FJH1

+ [6]

简介

S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methyluridine at position 1369 (Um1369) in the 16S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA (PubMed:25009282, PubMed:25074936, PubMed:35177605). This activity may require prior 2'-O-methylguanosine modification at position 1370 (Gm1370) by MRM3 (PubMed:35177605). Essential for late-stage assembly of mtLSU required for efficient translation of mitochondrial DNA encoded proteins; methyltransferase activity is not required for this function (PubMed:35177605). Essential for mitochondrial respiratory function (PubMed:35177605).

关联

100 项与 MRM2 相关的临床结果

登录后查看更多信息

100 项与 MRM2 相关的转化医学

登录后查看更多信息

0 项与 MRM2 相关的专利（医药）

登录后查看更多信息

项与 MRM2 相关的文献（医药）

2023-04-01·Journal of Medical Genetics

MRM2variants in families with complex dystonic syndromes: evidence for phenotypic heterogeneity

Article

作者: Sobreira, Nara ; Naz, Sadaf ; Hussain, Tooba ; Arif, Beenish ; Shafique, Anum ; Chu, Mary Lynn ; Moran, Ellen ; Lohmann, Katja ; Klein, Christine ; Zamora, Francisca Millan ; Wohler, Elizabeth

BackgroundDystonia involves repetitive movements and muscle contractions leading to abnormal postures. We investigated patients in two families, DYAF11 and M, exhibiting dystonic or involuntary movement disorders.MethodsClinical investigations were performed for all patients. Genetic analyses included genome-wide linkage analysis and exome sequencing followed by Sanger sequencing validation.MRM2-specific transcripts were analysed from participants’ blood samples in Family DYAF11 after cloning of gene-specific cDNA.ResultsFour affected siblings in Family DYAF11 had progressive dystonic features. Two patients in Family M exhibited a neurodevelopmental disorder accompanied by involuntary movements. In Family DYAF11, linkage was detected to the telomere at chromosome 7p22.3, spanning <2 Mb. Exome sequencing identified a donor splice-site variant, c.8+1G>T inMRM2,which segregated with the phenotype, corresponding to the linkage data since all affected individuals were homozygous while the obligate unaffected carriers were heterozygous for the variant. In theMRM2c.8+1G>T allele, an aberrant alternative acceptor splice-site located within exon 2 was used in a subset of the transcripts, creating a frameshift in the open reading frame. Exome sequencing in Family M revealed a rare missense variant c.242C>T, p.(Ala81Val), which affected a conserved amino acid.ConclusionsOur results expand the clinical and allelic spectrum ofMRM2variants. Previously, these descriptions were based on observations in a single patient, diagnosed with mitochondrial DNA depletion syndrome 17, in whom movement disorder was accompanied by recurrent strokes and epilepsy. We also demonstrate a subset of correctly spliced tt-agMRM2transcripts, raising the possibility to develop treatment by understanding the disease mechanism.

2022-02-01·Journal of Hazardous Materials

Insights into biodegradation mechanisms of triphenyl phosphate by a novel fungal isolate and its potential in bioremediation of contaminated river sediment

Article

作者: Wei Mao ; Mi Feng ; Jiahua Zhou ; Yushuo Guo ; Hao Wang ; Xiaolong Yu

In this study, Aspergillus sydowii FJH-1 isolated from soil was verified to be a novel triphenyl phosphate (TPhP) degrader. Biodegradation efficiency of TPhP by Aspergillus sydowii FJH-1 exceeded 90% within 6 days under the optimal conditions (pH 4-9, 30 ℃, initial concentration less than 20 mg/L). Proteomics analysis uncovered the proteins perhaps involved in hydrolysis, hydroxylation, methylation and sulfonation of TPhP and the primary intracellular adaptive responses of Aspergillus sydowii FJH-1 to TPhP stress. The expression of carboxylic ester hydrolase along with several thioredoxin- and glutathione-dependent oxidoreductases were induced to withstand the toxicity of TPhP. The presence of TPhP also caused obvious upregulation of proteins concerned with glycolysis, pentose phosphate pathway and tricarboxylic acid cycle. Data from toxicological tests confirmed that the cytotoxicity and phytotoxicity of TPhP was effectively decreased after treatment with Aspergillus sydowii FJH-1. Additionally, bioaugmentation with Aspergillus sydowii FJH-1 was available for promoting TPhP removal in real water and water-sediment system. Collectively, the present study offered a deeper insight into the biodegradation mechanism and pathway of TPhP by a newly screened fungal strain Aspergillus sydowii FJH-1 and validated the feasibility of applying this novel degrader in the bioremediation of TPhP-polluted matrices.

2021-01-11·Nucleic Acids Research2区 · 生物学

Human GTPBP5 is involved in the late stage of mitoribosome large subunit assembly

2区 · 生物学

ArticleOA

作者: Rosenberger, Florian A ; Wredenberg, Anna ; Busch, Jakob D ; Gopalakrishna, Shreekara ; Rorbach, Joanna ; Krüger, Annika ; Pearce, Sarah F ; Lopez Sanchez, Isabel G ; Li, Xinping ; Atanassov, Ilian ; Cipullo, Miriam

AbstractHuman mitoribosomes are macromolecular complexes essential for translation of 11 mitochondrial mRNAs. The large and the small mitoribosomal subunits undergo a multistep maturation process that requires the involvement of several factors. Among these factors, GTP-binding proteins (GTPBPs) play an important role as GTP hydrolysis can provide energy throughout the assembly stages. In bacteria, many GTPBPs are needed for the maturation of ribosome subunits and, of particular interest for this study, ObgE has been shown to assist in the 50S subunit assembly. Here, we characterize the role of a related human Obg-family member, GTPBP5. We show that GTPBP5 interacts specifically with the large mitoribosomal subunit (mt-LSU) proteins and several late-stage mitoribosome assembly factors, including MTERF4:NSUN4 complex, MRM2 methyltransferase, MALSU1 and MTG1. Interestingly, we find that interaction of GTPBP5 with the mt-LSU is compromised in the presence of a non-hydrolysable analogue of GTP, implying a different mechanism of action of this protein in contrast to that of other Obg-family GTPBPs. GTPBP5 ablation leads to severe impairment in the oxidative phosphorylation system, concurrent with a decrease in mitochondrial translation and reduced monosome formation. Overall, our data indicate an important role of GTPBP5 in mitochondrial function and suggest its involvement in the late-stage of mt-LSU maturation.

分析

对领域进行一次全面的分析。

或

查看完整样例数据

生物医药百科问答

全新生物医药AI Agent 覆盖科研全链路，让突破性发现快人一步

立即开始免费试用!

智慧芽新药情报库是智慧芽专为生命科学人士构建的基于AI的创新药情报平台，助您全方位提升您的研发与决策效率。

立即开始数据试用!

智慧芽新药库数据也通过智慧芽数据服务平台，以API或者数据包形式对外开放，助您更加充分利用智慧芽新药情报信息。