Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic Gene Ontology annotation based on Rhea mapping
Combined Automated Annotation using Multiple IEA Methods
TWINKLE Has 5' -> 3' DNA helicase activity and is specifically stimulated by mitochondrial single-stranded DNA-binding protein.
DNA and RNA binding by the mitochondrial lon protease is regulated by nucleotide and protein substrate.
Reconstitution of a minimal mtDNA replisome in vitro.
Modular architecture of the hexameric human mitochondrial DNA helicase.
The N-terminal domain of TWINKLE contributes to single-stranded DNA binding and DNA helicase activities.
The layered structure of human mitochondrial DNA nucleoids.
Twinkle mutations associated with autosomal dominant progressive external ophthalmoplegia lead to impaired helicase function and in vivo mtDNA replication stalling.
Human mitochondrial DNA helicase TWINKLE is both an unwinding and annealing helicase.
Alternative translation initiation augments the human mitochondrial proteome.
The hexameric structure of the human mitochondrial replicative helicase Twinkle.
Regulation of DNA replication at the end of the mitochondrial D-loop involves the helicase TWINKLE and a conserved sequence element.
Biochemical Characterization of the Human Mitochondrial Replicative Twinkle Helicase: SUBSTRATE SPECIFICITY, DNA BRANCH MIGRATION, AND ABILITY TO OVERCOME BLOCKADES TO DNA UNWINDING.
Architecture of the human interactome defines protein communities and disease networks.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
Implications of Membrane Binding by the Fe-S Cluster-Containing N-Terminal Domain in the Drosophila Mitochondrial Replicative DNA Helicase.
Structural insight and characterization of human Twinkle helicase in mitochondrial disease.
Expression of TWINKLE (TWNK, PEO1)
LONP1 degrades mitochondrial matrix proteins
LONP1 binds mitochondrial matrix proteins
POLG:POLG2 and TWNK (PEO1) bind mitochondrial DNA:RNA primer to form H strand replisome
POLG in the replisome polymerizes the H strand
POLRMT and POLG bind the mitochondrial L strand replication origin (OriL)
POLRMT polymerizes RNA primer for mitochondrial L strand replication
TWNK (PEO1) unwinds double-stranded mitochondrial DNA at the replication fork
SSBP1 binds the displaced parental H strand
POLG in the replisome polymerizes the L strand
RNASEH1 cleaves RNA primer from nascent H strand, leaving RNA dinucleotides
TWINKLE is an essential mitochondrial helicase required for synthesis of nascent D-loop strands and complete mtDNA replication.
Modeling pathogenic mutations of human twinkle in Drosophila suggests an apoptosis role in response to mitochondrial defects.
Manual literature synthesis for TWNK