Target intelligence / Profile preview

Probable ATP-dependent RNA helicase DDX28 (DDX28)

Target
DDX28
Molecular classification
Enzyme, RNA helicase (DEAD-box family), Mitochondrial matrix protein
01

Overview

Probable ATP-dependent RNA helicase DDX28 is a member of the DEAD-box family of RNA helicases, characterized by the conserved DEAD motif (Asp-Glu-Ala-Asp). It is an enzyme with RNA-dependent ATPase and helicase activities, localized primarily in the mitochondrial matrix, where it plays an essential role in the biogenesis of the mitochondrial large ribosomal subunit (mt-LSU)[3]. DDX28 interacts directly with mitochondrial 16S rRNA, and its silencing leads to impaired mt-LSU assembly, reduced mitochondrial protein synthesis, and deficient assembly of oxidative phosphorylation complexes, resulting in compromised cellular respiration[1][3]. Its activity is indispensable for normal mitochondrial translation and energy metabolism. Mutations or deficiencies in DDX28 are associated with diseases such as Spastic Paraplegia 7 (autosomal recessive) and Perrault syndrome[3]. DDX28 is not currently considered a therapeutic target, and no interacting drugs or mechanisms of action for drug targeting are reported.

Other names
DEAD-box helicase 28DDX28MDDX28FLJ11282Mitochondrial DEAD box protein 28DEAD (Asp-Glu-Ala-Asp) box polypeptide 28DEAD/H (Asp-Glu-Ala-Asp/His) box polypeptide 28
02

Biological functions

RNA metabolismBiogenesis of the mitochondrial large ribosomal subunit (mt-LSU)ATP-dependent RNA helicase activityRNA processing and transportRibosome assembly (mitoribosome)Maintenance of mitochondrial translation machinery
03

Disease associations

Spastic paraplegia 7, autosomal recessivePerrault syndromeOther (potentially involved in mitochondrial disorders due to its key role in mitochondrial ribosome assembly and function)
04

Safety considerations

Disruption can impair mitochondrial function and protein synthesis, leading to decreased oxidative phosphorylation and energy productionKnockdown leads to failure in assembly of mitochondrial OXPHOS complexes, respiratory deficiency, and cellular dysfunction

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