HEMK1

Last update 08 May 2025

Basic Info

Synonyms

HEMK, HemK methyltransferase family member 1, HEMK1

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Introduction

N5-glutamine methyltransferase responsible for the methylation of the glutamine residue in the universally conserved GGQ motif of the mitochondrial translation release factors MTRF1, MTRF1L, MRPL58/ICT1 and MTRFR.

100 Clinical Results associated with HEMK1

100 Translational Medicine associated with HEMK1

0 Patents (Medical) associated with HEMK1

Literatures (Medical) associated with HEMK1

01 Apr 2025·Molecular Cell

Modulation of protein activity by small RNA base pairing internal to coding sequences

Article

Author: Storz, Gisela ; Alaniz, Miranda M ; Esnault, Caroline ; Zhang, Hongen ; Rodnina, Marina V ; Samatova, Ekaterina ; Zhong, Aoshu ; Dale, Ryan K ; Thongdee, Narumon

Most characterized interactions between bacterial small RNAs (sRNAs) and their target mRNAs occur near ribosome binding sites, resulting in changes in translation initiation or target mRNA decay. To understand the consequences of sRNA pairing internal to coding sequences detected by global RNA-RNA interactome approaches, we examined the impact of sRNA overexpression on seven target proteins. Overexpression of the sRNA led to decreased target protein levels for two pairs, but there were no differences for the others. By further examining ArcZ-ligA and ArcZ-hemK, we discovered that ArcZ pairing with the mRNAs leads to translation pausing and increased protein activity. A ligA point mutation that eliminates sRNA pairing resulted in increased sensitivity to DNA damage, revealing the physiological consequences of the regulation. Thus, regulatory RNA pairing in coding sequences can locally slow translation elongation, likely impacting co-translational protein folding and allowing improved incorporation of co-factors or more optimal folding under specific conditions.

01 Jul 2024·Molecular Plant Pathology

A cyclic di‐GMP‐binding adaptor protein interacts with a N5‐glutamine methyltransferase to regulate the pathogenesis in Xanthomonas citri subsp. citri

Article

Author: Liang, Zhao‐Xun ; Cheang, Qing Wei ; Shi, Yu ; Zhao, Xiaoyan ; Xu, Zeling ; Cheng, Tianfang ; Wang, Junxia ; Xu, Linghui

AbstractThe second messenger cyclic diguanylate monophosphate (c‐di‐GMP) regulates a wide range of bacterial behaviours through diverse mechanisms and binding receptors. Single‐domain PilZ proteins, the most widespread and abundant known c‐di‐GMP receptors in bacteria, act as trans‐acting adaptor proteins that enable c‐di‐GMP to control signalling pathways with high specificity. This study identifies a single‐domain PilZ protein, XAC3402 (renamed N5MapZ), from the phytopathogen Xanthomonas citri subsp. citri (Xcc), which modulates Xcc virulence by directly interacting with the methyltransferase HemK. Through yeast two‐hybrid, co‐immunoprecipitation and immunofluorescent staining, we demonstrated that N5MapZ and HemK interact directly under both in vitro and in vivo conditions, with the strength of the protein–protein interaction decreasing at high c‐di‐GMP concentrations. This finding distinguishes N5MapZ from other characterized single‐domain PilZ proteins, as it was previously known that c‐di‐GMP enhances the interaction between those single‐domain PilZs and their protein partners. This observation is further supported by the fact that the c‐di‐GMP binding‐defective mutant N5MapZR10A can interact with HemK to inhibit the methylation of the class 1 translation termination release factor PrfA. Additionally, we found that HemK plays an important role in Xcc pathogenesis, as the deletion of hemK leads to extensive phenotypic changes, including reduced virulence in citrus plants, decreased motility, production of extracellular enzymes and stress tolerance. Gene expression analysis has revealed that c‐di‐GMP and the HemK‐mediated pathway regulate the expression of multiple virulence effector proteins, uncovering a novel regulatory mechanism through which c‐di‐GMP regulates Xcc virulence by mediating PrfA methylation via the single‐domain PilZ adaptor protein N5MapZ.

30 Jul 2022·Journal of Industrial Microbiology and BiotechnologyQ3 · ENGINEERING & TECHNOLOGY

Characterization and utilization of methyltransferase for apramycin production in Streptoalloteichus tenebrarius

Q3 · ENGINEERING & TECHNOLOGY

Article

Author: Liu, Yu ; Sun, Junyang ; Ni, Xianpu ; Yan, Danyang ; Gao, Hongjing ; Xia, Huanzhang

AbstractA structurally unique aminoglycoside produced in Streptoalloteichus tenebrarius, Apramycin is used in veterinary medicine or the treatment of Salmonella, Escherichia coli, and Pasteurella multocida infections. Although apramycin was discovered nearly 50 years ago, many biosynthetic steps of apramycin remain unknown. In this study, we identified a HemK family methyltransferase, AprI, to be the 7’-N-methyltransferase in apramycin biosynthetic pathway. Biochemical experiments showed that AprI converted demethyl-aprosamine to aprosamine. Through gene disruption of aprI, we identified a new aminoglycoside antibiotic demethyl-apramycin as the main product in aprI disruption strain. The demethyl-apramycin is an impurity in apramycin product. In addition to demethyl-apramycin, carbamyltobramycin is another major impurity. However, unlike demethyl-apramycin, tobramycin is biosynthesized by an independent biosynthetic pathway in S. tenebrarius. The titer and rate of apramycin were improved by overexpression of the aprI and disruption of the tobM2, which is a crucial gene for tobramycin biosynthesis. The titer of apramycin increased from 2227 ± 320 mg/L to 2331 ± 210 mg/L, while the titer of product impurity demethyl-apramycin decreased from 196 ± 36 mg/L to 51 ± 9 mg/L. Moreover, the carbamyltobramycin titer of the wild-type strain was 607 ± 111 mg/L and that of the engineering strain was null. The rate of apramycin increased from 68% to 87% and that of demethyl-apramycin decreased from 1.17% to 0.34%.

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HEMK1

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