TSR3: A Potential Drug Target and Biomarker for Acyl-CoA Transferase Ribosome Maturation Factor

Target Name: TSR3

NCBI ID: G115939

TSR3: A Potential Drug Target and Biomarker for Acyl-CoA Transferase Ribosome Maturation Factor

Abstract:

Acyl-CoA transferase (ACP) ribosome maturation factor (TSR3) is a protein that plays a crucial role in the regulation of protein synthesis in eukaryotic cells. The dysfunction of TSR3 has been implicated in various diseases, including obesity, diabetes, and neurodegenerative disorders . This article aims to provide an overview of TSR3, its functions, and potential as a drug target or biomarker.

Introduction:

Protein synthesis is a critical process that occurs in all living organisms, and it is supported by a complex network of enzymes and factors. The acyl-CoA transferase (ACP) ribosome maturation factor (TSR3) is one of the key enzymes involved in this process . TSR3 is a protein that functions as a critical regulator of protein synthesis, and its dysfunction has been implicated in various diseases.

History of TSR3:

TSR3 was first identified in the 1970s as a protein that is expressed in the cytoplasm of mammalian cells. Since then, numerous studies have demonstrated that TSR3 plays a crucial role in regulating protein synthesis in eukaryotic cells. TSR3 has been shown to regulate the translation of mRNAs, interact with factors such as factors that influence post-transcriptional modification (PTM), and modulate the activity of other enzymes involved in the protein synthesis pathway.

Function of TSR3:

TSR3 is involved in the regulation of several key steps in the protein synthesis pathway, including the initiation of translation, the addition of exons to pre-mRNA, the modification of pre-mRNA, and the termination of translation. TSR3 has been shown to interact with several factors that influence these processes, including the 40S ribosome (40SrRNA), the 28S ribosome (28SrRNA), and the splicing machinery.

TSR3 has also been shown to play a key role in the regulation of post-transcriptional modification (PTM) of mRNAs. PTM is a critical process that occurs during the translation of mRNAs, and it includes the addition of various modifications, such as splicing, splicing, and modification of the 3' end. TSR3 has been shown to regulate the activity of enzymes involved in PTM and to interact with factors that influence the level of PTM on mRNAs.

TSR3 has also been shown to play a crucial role in the regulation of the activity of other enzymes involved in the protein synthesis pathway. TSR3 has been shown to interact with factors involved in the translation of mRNAs, such as the TOR kinase, and it has has also been shown to regulate the activity of enzymes involved in the folding and localization of proteins.

Potential as a Drug Target or Biomarker:

The dysfunction of TSR3 has been implicated in various diseases, including obesity, diabetes, and neurodegenerative disorders. The potential of TSR3 as a drug target or biomarker is under investigation in these diseases.

In the context of obesity, TSR3 has been shown to play a crucial role in the regulation of energy metabolism and to interact with factors that influence lipid metabolism. The dysfunction of TSR3 has been implicated in the development of obesity, and TSR3 has been shown to be involved in the regulation of the activity of enzymes involved in lipid metabolism. Therefore, TSR3 may be an attractive target for interventions aimed at reducing obesity.

In the context of diabetes, TSR3 has been shown to play a crucial role in the regulation of insulin sensitivity and to interact with factors that influence glucose metabolism. The dysfunction of TSR3 has

Protein Name: TSR3 Ribosome Maturation Factor

Functions: Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine at position 1248 (Psi1248) in 18S rRNA (Probable). It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA (Probable)

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