PDSS1

From Wikipedia, the free encyclopedia

Prenyl (decaprenyl) diphosphate synthase, subunit 1

Identifiers

PDSS1; COQ1; MGC70953; RP13-16H11.3; TPRT; TPT; hDPS1

External IDs

OMIM: 607429 MGI: 1889278 HomoloGene: 5353

Gene ontology
Molecular Function:	• trans-hexaprenyltranstransferase activity • transferase activity • protein heterodimerization activity • trans-octaprenyltranstransferase activity
Biological Process:	• ubiquinone biosynthetic process • isoprenoid biosynthetic process • protein heterotetramerization

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_014317 (mRNA)
NP_055132 (protein)

NM_019501 (mRNA)
NP_062374 (protein)

Location

Chr 10: 27.03 - 27.08 Mb

Chr 2: 22.75 - 22.77 Mb

Pubmed search

[1]

[2]

Prenyl (decaprenyl) diphosphate synthase, subunit 1, also known as PDSS1, is a human gene.^[1]

The protein encoded by this gene is an enzyme that elongates the prenyl side-chain of coenzyme Q, or ubiquinone, one of the key elements in the respiratory chain. The gene product catalyzes the formation of all trans-polyprenyl pyrophosphates from isopentyl diphosphate in the assembly of polyisoprenoid side chains, the first step in coenzyme Q biosynthesis. The protein may be peripherally associated with the inner mitochondrial membrane, though no transit peptide has been definitively identified to date.^[1]

[edit] References

^ ^a ^b Entrez Gene: PDSS1 prenyl (decaprenyl) diphosphate synthase, subunit 1.

[edit] Further reading

Appelkvist EL, Aberg F, Guan Z, et al. (1995). "Regulation of coenzyme Q biosynthesis.". Mol. Aspects Med. 15 Suppl: s37-46. PMID 7752843.
Runquist M, Ericsson J, Thelin A, et al. (1994). "Isoprenoid biosynthesis in rat liver mitochondria. Studies on farnesyl pyrophosphate synthase and trans-prenyltransferase.". J. Biol. Chem. 269 (8): 5804-9. PMID 8119922.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171-4. PMID 8125298.
Teclebrhan H, Olsson J, Swiezewska E, Dallner G (1993). "Biosynthesis of the side chain of ubiquinone:trans-prenyltransferase in rat liver microsomes.". J. Biol. Chem. 268 (31): 23081-6. PMID 8226825.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149-56. PMID 9373149.
Rötig A, Appelkvist EL, Geromel V, et al. (2000). "Quinone-responsive multiple respiratory-chain dysfunction due to widespread coenzyme Q10 deficiency.". Lancet 356 (9227): 391-5. PMID 10972372.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932.
Deloukas P, Earthrowl ME, Grafham DV, et al. (2004). "The DNA sequence and comparative analysis of human chromosome 10.". Nature 429 (6990): 375-81. doi:10.1038/nature02462. PMID 15164054.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334.
Saiki R, Nagata A, Kainou T, et al. (2005). "Characterization of solanesyl and decaprenyl diphosphate synthases in mice and humans.". FEBS J. 272 (21): 5606-22. doi:10.1111/j.1742-4658.2005.04956.x. PMID 16262699.
Mollet J, Giurgea I, Schlemmer D, et al. (2007). "Prenyldiphosphate synthase, subunit 1 (PDSS1) and OH-benzoate polyprenyltransferase (COQ2) mutations in ubiquinone deficiency and oxidative phosphorylation disorders.". J. Clin. Invest. 117 (3): 765-72. doi:10.1172/JCI29089. PMID 17332895.