From Wikipedia, the free encyclopedia
DCPS
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases DCPS, DCS1, HINT-5, HINT5, HSL1, ARS, HSPC015, decapping enzyme, scavenger
External IDs OMIM: 610534; MGI: 1916555; HomoloGene: 32202; GeneCards: DCPS; OMA: DCPS - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_014026
NM_001350236

NM_027030

RefSeq (protein)

NP_054745
NP_001337165

NP_081306

Location (UCSC) Chr 11: 126.3 – 126.35 Mb Chr 9: 35.04 – 35.09 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse
Scavenger mRNA decapping enzyme (DcpS) N-terminal
crystal structure of mrna decapping enzyme (dcps) from mus musculus at 1.83 a resolution
Identifiers
SymbolDcpS
Pfam PF05652
InterPro IPR008594
SCOP2 1st4 / SCOPe / SUPFAM
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary
Scavenger mRNA decapping enzyme C-term binding
Identifiers
SymbolDcpS_C
Pfam PF11969
Pfam clan CL0265
SCOP2 1st4 / SCOPe / SUPFAM
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

Scavenger mRNA-decapping enzyme DcpS is a protein that in humans is encoded by the DCPS gene. [5] [6] [7]

The scavenger mRNA decapping enzymes include Dcp2 and DcpS. DcpS is a scavenger pyrophosphatase that hydrolyses the residual cap structure following 3' to 5' mRNA degradation. DcpS uses cap dinucleotides or capped oligonucleotides as substrates to release m(7)GMP (N7-methyl GMP), while Dcp2 uses capped mRNA as a substrate in order to hydrolyse the cap to release m(7)GDP (N7-methyl GDP). [8] The association of DcpS with 3' to 5' exonuclease exosome components suggests that these two activities are linked and there is a coupled exonucleolytic decay-dependent decapping pathway. The family contains a histidine triad (HIT) sequence in its C-terminal domain, with three histidines separated by hydrophobic residues. [9] The central histidine within the DcpS HIT motif is critical for decapping activity and defines the HIT motif as a new mRNA decapping domain, making DcpS the first member of the HIT family of proteins with a defined biological function.

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000110063Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000032040Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Liu H, Rodgers ND, Jiao X, Kiledjian M (Aug 2002). "The scavenger mRNA decapping enzyme DcpS is a member of the HIT family of pyrophosphatases". EMBO J. 21 (17): 4699–4708. doi: 10.1093/emboj/cdf448. PMC  126188. PMID  12198172.
  6. ^ van Dijk E, Le Hir H, Seraphin B (Oct 2003). "DcpS can act in the 5'-3' mRNA decay pathway in addition to the 3'-5' pathway". Proc Natl Acad Sci U S A. 100 (21): 12081–12086. Bibcode: 2003PNAS..10012081V. doi: 10.1073/pnas.1635192100. PMC  218716. PMID  14523240.
  7. ^ "Entrez Gene: DCPS decapping enzyme, scavenger".
  8. ^ Liu H, Kiledjian M (February 2006). "Decapping the message: a beginning or an end". Biochem. Soc. Trans. 34 (Pt 1): 35–8. doi: 10.1042/BST20060035. PMID  16246173.
  9. ^ Han GW, Schwarzenbacher R, McMullan D, Abdubek P, Ambing E, Axelrod H, Biorac T, Canaves JM, Chiu HJ, Dai X, Deacon AM, DiDonato M, Elsliger MA, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Haugen J, Hornsby M, Jaroszewski L, Klock HE, Koesema E, Kreusch A, Kuhn P, Lesley SA, McPhillips TM, Miller MD, Moy K, Nigoghossian E, Paulsen J, Quijano K, Reyes R, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, Wilson IA (September 2005). "Crystal structure of an Apo mRNA decapping enzyme (DcpS) from Mouse at 1.83 A resolution". Proteins. 60 (4): 797–802. doi: 10.1002/prot.20467. PMID  16001405. S2CID  20494085.

Further reading

External links

  • PDBe-KB provides an overview of all the structure information available in the PDB for Human m7GpppX diphosphatase (DCPS)
This article incorporates text from the public domain Pfam and InterPro: IPR008594


From Wikipedia, the free encyclopedia
DCPS
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases DCPS, DCS1, HINT-5, HINT5, HSL1, ARS, HSPC015, decapping enzyme, scavenger
External IDs OMIM: 610534; MGI: 1916555; HomoloGene: 32202; GeneCards: DCPS; OMA: DCPS - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_014026
NM_001350236

NM_027030

RefSeq (protein)

NP_054745
NP_001337165

NP_081306

Location (UCSC) Chr 11: 126.3 – 126.35 Mb Chr 9: 35.04 – 35.09 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse
Scavenger mRNA decapping enzyme (DcpS) N-terminal
crystal structure of mrna decapping enzyme (dcps) from mus musculus at 1.83 a resolution
Identifiers
SymbolDcpS
Pfam PF05652
InterPro IPR008594
SCOP2 1st4 / SCOPe / SUPFAM
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary
Scavenger mRNA decapping enzyme C-term binding
Identifiers
SymbolDcpS_C
Pfam PF11969
Pfam clan CL0265
SCOP2 1st4 / SCOPe / SUPFAM
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

Scavenger mRNA-decapping enzyme DcpS is a protein that in humans is encoded by the DCPS gene. [5] [6] [7]

The scavenger mRNA decapping enzymes include Dcp2 and DcpS. DcpS is a scavenger pyrophosphatase that hydrolyses the residual cap structure following 3' to 5' mRNA degradation. DcpS uses cap dinucleotides or capped oligonucleotides as substrates to release m(7)GMP (N7-methyl GMP), while Dcp2 uses capped mRNA as a substrate in order to hydrolyse the cap to release m(7)GDP (N7-methyl GDP). [8] The association of DcpS with 3' to 5' exonuclease exosome components suggests that these two activities are linked and there is a coupled exonucleolytic decay-dependent decapping pathway. The family contains a histidine triad (HIT) sequence in its C-terminal domain, with three histidines separated by hydrophobic residues. [9] The central histidine within the DcpS HIT motif is critical for decapping activity and defines the HIT motif as a new mRNA decapping domain, making DcpS the first member of the HIT family of proteins with a defined biological function.

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000110063Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000032040Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Liu H, Rodgers ND, Jiao X, Kiledjian M (Aug 2002). "The scavenger mRNA decapping enzyme DcpS is a member of the HIT family of pyrophosphatases". EMBO J. 21 (17): 4699–4708. doi: 10.1093/emboj/cdf448. PMC  126188. PMID  12198172.
  6. ^ van Dijk E, Le Hir H, Seraphin B (Oct 2003). "DcpS can act in the 5'-3' mRNA decay pathway in addition to the 3'-5' pathway". Proc Natl Acad Sci U S A. 100 (21): 12081–12086. Bibcode: 2003PNAS..10012081V. doi: 10.1073/pnas.1635192100. PMC  218716. PMID  14523240.
  7. ^ "Entrez Gene: DCPS decapping enzyme, scavenger".
  8. ^ Liu H, Kiledjian M (February 2006). "Decapping the message: a beginning or an end". Biochem. Soc. Trans. 34 (Pt 1): 35–8. doi: 10.1042/BST20060035. PMID  16246173.
  9. ^ Han GW, Schwarzenbacher R, McMullan D, Abdubek P, Ambing E, Axelrod H, Biorac T, Canaves JM, Chiu HJ, Dai X, Deacon AM, DiDonato M, Elsliger MA, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Haugen J, Hornsby M, Jaroszewski L, Klock HE, Koesema E, Kreusch A, Kuhn P, Lesley SA, McPhillips TM, Miller MD, Moy K, Nigoghossian E, Paulsen J, Quijano K, Reyes R, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, Wilson IA (September 2005). "Crystal structure of an Apo mRNA decapping enzyme (DcpS) from Mouse at 1.83 A resolution". Proteins. 60 (4): 797–802. doi: 10.1002/prot.20467. PMID  16001405. S2CID  20494085.

Further reading

External links

  • PDBe-KB provides an overview of all the structure information available in the PDB for Human m7GpppX diphosphatase (DCPS)
This article incorporates text from the public domain Pfam and InterPro: IPR008594



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