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HLCS encodes an enzyme that catalyzes the binding of biotin to carboxylases and histones.
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The function of HCS and biotin in metabolism and human disease, a putative role for the enzyme in histone biotinylation, and its participation as a nuclear factor in chromatin dynamics is discussed.
The transcriptional function of HCS was shown by in vitro pull down and in vivo co-immunoprecipitation assays to depend on its interaction with the histone deacetylases HDAC1 (zeige HDAC1 ELISA Kits), HDAC2 (zeige HDAC2 ELISA Kits) and HDAC7 (zeige HDAC7 ELISA Kits)
Data suggest that direct interactions of HLCS (holocarboxylase synthetase) with NCOR1 (nuclear receptor corepressor 1 (zeige NCOR1 ELISA Kits)) and HDAC1 (histone deacetylase 1 (zeige HDAC1 ELISA Kits)) contribute toward transcriptional repression of repeats, presumably increasing genome stability.
study characterizes three functional promoters in the human HLCS gene
HLCS interacts physically with the DNA methyltransferase (zeige DNMT1 ELISA Kits) DNMT1 (zeige DNMT1 ELISA Kits) and the methyl CpG binding protein MeCP2 to facilitate the binding of HLCS to chromatin.
This study showed that modification of HSP72 (zeige HSPA1A ELISA Kits) and demonstrated that binding of biotin to extracellular HSP72 (zeige HSPA1A ELISA Kits) prepares cells for a strong immune response.
individuals with HLCS SNPs may benefit from supplemental biotin, yet to different extents depending on the genotype
HLCS methionine-58 is a functional translation start site in human cells.
Holocarboxylase synthetase interacts directly with histone H3 (zeige HIST3H3 ELISA Kits), causing biotinylation of lysine K9 and K18 (zeige KRT18 ELISA Kits).
Mutation analysis by polymerase chain reaction-sequencing of the entire coding region of the HLCS gene revealed the c.1522C>T (p.R508W) mutation in six of the eight mutant alleles. suggests it as the most common mutation in the Thai population
This gene encodes an enzyme that catalyzes the binding of biotin to carboxylases and histones. The protein plays an important role in gluconeogenesis, fatty acid synthesis and branched chain amino acid catabolism. Defects in this gene are the cause of holocarboxylase synthetase deficiency. Multiple alternatively spliced variants, encoding the same protein, have been identified.
biotin apo-protein ligase
, biotin- [propriony-Coenzyme A-carboxylase (ATP-hydrolysing)] ligase
, biotin--protein ligase
, biotin--[acetyl-CoA-carboxylase] ligase
, biotin--[methylcrotonoyl-CoA-carboxylase] ligase
, biotin--[methylmalonyl-CoA-carboxytransferase] ligase
, holocarboxylase synthetase (biotin-(proprionyl-Coenzyme A-carboxylase (ATP-hydrolysing)) ligase)
, holocarboxylase synthetase (biotin- [propriony-Coenzyme A-carboxylase (ATP-hydrolysing)] ligase)