Gene Information
- Official Symbol: PDF
- Official Name: peptide deformylase, mitochondrial
- Aliases and Previous Symbols: N/A
- Entrez ID: 64146
- UniProt: Q9HBH1
- Interactions: BioGRID
- PubMed articles: Open PubMed
- OMIM: Open OMIM
Function Summary
- Entrez Summary: Protein synthesis proceeds after formylation of methionine by methionyl-tRNA formyl transferase (FMT) and transfer of the charged initiator f-met tRNA to the ribosome. In eubacteria and eukaryotic organelles the product of this gene, peptide deformylase (PDF), removes the formyl group from the initiating methionine of nascent peptides. In eubacteria, deformylation of nascent peptides is required for subsequent cleavage of initiating methionines by methionine aminopeptidase. The discovery that a natural inhibitor of PDF, actinonin, acts as an antimicrobial agent in some bacteria has spurred intensive research into the design of bacterial-specific PDF inhibitors. In human cells, only mitochondrial proteins have N-formylation of initiating methionines. Protein inhibitors of PDF or siRNAs of PDF block the growth of cancer cell lines but have no effect on normal cell growth. In humans, PDF function may therefore be restricted to rapidly growing cells. [provided by RefSeq, Nov 2008].
- UniProt Summary: Removes the formyl group from the N-terminal Met of newly synthesized proteins. {ECO:0000250}.
CRISPR Data
Essentiality in NALM6
- Essentiality Rank: 12349
- Expression level (log2 read counts): 4.27
PDF Expression in NALM6 Cells: 4.27
