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DCPS may refer to:

  • Dahlem Centre of Plant Sciences, a research focus area of Freie Universität Berlin, Germany
  • DCPS (gene), a human gene that encodes the scavenger mRNA-decapping enzyme DcpS
  • DCPS (TV channel), a public-access television station based in Duval County, Florida
  • DECprint Supervisor, (DCPS) developed by DEC, Digital Equipment Corporation - The DECprint Supervisor software allows people to use and manage networked PostScript printers.
  • Distributed cyber-physical system, a cyber-physical system which involves extensive distributed computation
  • District of Columbia Public Schools, which operates the public schools in Washington, DC
  • Dominican Convent Primary School, Bulawayo, an independent school in Bulawayo, Zimbabwe
  • Dulwich College Preparatory School, a private school in the United Kingdom
  • Duval County Public Schools, which operates public schools in Jacksonville, Florida
  • M7GpppX diphosphatase, an enzyme

It might also be used for

  • Miami-Dade County Public Schools
DCPS (gene)

Scavenger mRNA-decapping enzyme DcpS is a protein that in humans is encoded by the DCPS gene.

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). 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. 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.