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tRNA methyltransferase 6 non-catalytic subunit (TRMT6)

Target
TRMT6
Molecular classification
Enzyme (Methyltransferase complex, non-catalytic subunit), Other (RNA modification complex member)
01

Overview

TRMT6 is the non-catalytic subunit of the tRNA (adenine^58^-N1)-methyltransferase complex, which forms a heterodimer with the catalytic subunit TRMT61A[3]. This complex catalyzes the methylation of adenine 58 in the T-loop of tRNA (m^1^A^58^)—a conserved modification essential for proper tRNA folding and function. TRMT6 lacks a functional methyltransferase active site but is necessary for tRNA binding and substrate specificity, facilitating the positioning of substrate tRNA for modification by TRMT61A. Disruption of TRMT6 impairs m^1^A^58^ formation and tRNA stability, impacting translation efficiency and fidelity. Deficiencies or misregulation in the complex have been linked to defects in protein biosynthesis and, in model organisms, to abnormal cellular growth and disease phenotypes[3]. Summary: - The phrase "tRNA methyltransferase 6 non-catalytic subunit" most accurately refers to TRMT6, the non-catalytic part of a methyltransferase complex (TRMT6/TRMT61A) in humans responsible for a specific tRNA adenine methylation. It is not a receptor, but a critical component required for enzymatic tRNA modification activity[3]. - The molecule is essential for cell biology but not currently targeted by drugs. - The term is somewhat imprecise—human naming conventions prefer “TRMT6” (or for the complex, “tRNA (adenine(58)-N1)-methyltransferase complex”)[3].

Other names
TRM6 (yeast homolog)TRMT6 (human gene/protein)tRNA (adenine(58)-N1)-methyltransferase non-catalytic subunit TRMT6Gcd10 in yeast
02

Mechanism of action

Not applicable for direct drug action, but genetic knockdown or mutation ablates tRNA m^1A^58 methylation, disrupting normal RNA processing[3].

03

Biological functions

tRNA modificationPost-transcriptional gene regulationTranslation fidelity
04

Disease associations

Cancer (Misregulation of tRNA methylation enzymes implicated in cancer and metabolic diseases[2])Other (General roles in translational regulation may indirectly affect multiple diseases)
05

Safety considerations

Unclear, as direct inhibition has not been clinically attempted and is likely cytotoxic due to requirement for normal translation; knockout causes tRNA maturation and translation defects[3].
06

Interacting drugs

None currently approved or in clinical use. As of the current knowledge, there are no drugs known to directly inhibit or interact with TRMT6 in humans.
07

Biomarkers

None in clinical use, but altered expression or mutation of TRMT6 complex members is under research as a potential biomarker for translational dysregulation[2].

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