| CircRNA HLCS regulates lens epithelial cell apoptosis via miR-338-3p/BPNT1 axis. | CircRNA HLCS regulates lens epithelial cell apoptosis via miR-338-3p/BPNT1 axis.
Sun L, Li F, Bai S, Bi C. | 03/19/2024 |
| Biotin protein ligase as you like it: Either extraordinarily specific or promiscuous protein biotinylation. | Biotin protein ligase as you like it: Either extraordinarily specific or promiscuous protein biotinylation.
Cronan JE., | 03/8/2024 |
| Clinical, biochemical, and genetic analysis of 28 Chinese patients with holocarboxylase synthetase deficiency. | Clinical, biochemical, and genetic analysis of 28 Chinese patients with holocarboxylase synthetase deficiency.
Ling S, Qiu W, Zhang H, Liang L, Lu D, Chen T, Zhan X, Wang Y, Gu X, Han L., Free PMC Article | 08/9/2023 |
| 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. | Holocarboxylase Synthetase: A Moonlighting Transcriptional Coregulator of Gene Expression and a Cytosolic Regulator of Biotin Utilization.
León-Del-Río A, Valadez-Graham V, Gravel RA. | 10/7/2017 |
| 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, HDAC2 and HDAC7 | Holocarboxylase synthetase acts as a biotin-independent transcriptional repressor interacting with HDAC1, HDAC2 and HDAC7.
Trujillo-Gonzalez I, Cervantes-Roldan R, Gonzalez-Noriega A, Michalak C, Reyes-Carmona S, Barrios-Garcia T, Meneses-Morales I, Leon-Del-Rio A. | 02/14/2015 |
| Data suggest that direct interactions of HLCS (holocarboxylase synthetase) with NCOR1 (nuclear receptor corepressor 1) and HDAC1 (histone deacetylase 1) contribute toward transcriptional repression of repeats, presumably increasing genome stability. | Holocarboxylase synthetase interacts physically with nuclear receptor co-repressor, histone deacetylase 1 and a novel splicing variant of histone deacetylase 1 to repress repeats.
Liu D, Zempleni J., Free PMC Article | 09/27/2014 |
| study characterizes three functional promoters in the human HLCS gene | Three promoters regulate the transcriptional activity of the human holocarboxylase synthetase gene.
Xia M, Malkaram SA, Zempleni J., Free PMC Article | 05/17/2014 |
| HLCS interacts physically with the DNA methyltransferase DNMT1 and the methyl CpG binding protein MeCP2 to facilitate the binding of HLCS to chromatin. | Holocarboxylase synthetase synergizes with methyl CpG binding protein 2 and DNA methyltransferase 1 in the transcriptional repression of long-terminal repeats.
Xue J, Wijeratne SS, Zempleni J., Free PMC Article | 03/22/2014 |
| This study showed that modification of HSP72 and demonstrated that binding of biotin to extracellular HSP72 prepares cells for a strong immune response. | Holocarboxylase synthetase catalyzes biotinylation of heat shock protein 72, thereby inducing RANTES expression in HEK-293 cells.
Xue J, Zhou J, Zempleni J., Free PMC Article | 02/15/2014 |
| individuals with HLCS SNPs may benefit from supplemental biotin, yet to different extents depending on the genotype | Effects of single-nucleotide polymorphisms in the human holocarboxylase synthetase gene on enzyme catalysis.
Esaki S, Malkaram SA, Zempleni J., Free PMC Article | 08/4/2012 |
| HLCS methionine-58 is a functional translation start site in human cells. | Human holocarboxylase synthetase with a start site at methionine-58 is the predominant nuclear variant of this protein and has catalytic activity.
Bao B, Wijeratne SS, Rodriguez-Melendez R, Zempleni J., Free PMC Article | 10/15/2011 |
| Holocarboxylase synthetase interacts directly with histone H3, causing biotinylation of lysine K9 and K18. | Holocarboxylase synthetase is a chromatin protein and interacts directly with histone H3 to mediate biotinylation of K9 and K18.
Bao B, Pestinger V, Hassan YI, Borgstahl GE, Kolar C, Zempleni J., Free PMC Article | 08/20/2011 |
| 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 | Holocarboxylase synthetase deficiency: novel clinical and molecular findings.
Tammachote R, Janklat S, Tongkobpetch S, Suphapeetiporn K, Shotelersuk V. | 10/23/2010 |
| The results of this study suggest that miR-539 is among the factors sensing biotin and regulating holocarboxylase synthetase expression. | Biotin regulates the expression of holocarboxylase synthetase in the miR-539 pathway in HEK-293 cells.
Bao B, Rodriguez-Melendez R, Wijeratne SS, Zempleni J., Free PMC Article | 09/20/2010 |
| Data suggest that the N-terminal domain of hHCS recognizes the charged region of biotin acceptor protein, distinctly from the recognition by the catalytic domain. | The N-terminal domain of human holocarboxylase synthetase facilitates biotinylation via direct interaction with the substrate protein.
Lee CK, Cheong C, Jeon YH. | 05/10/2010 |
| the localisation of HCS and its isoforms | Holocarboxylase synthetase: correlation of protein localisation with biological function.
Bailey LM, Wallace JC, Polyak SW. | 04/12/2010 |
| The mutations R508W and V363D of holocarboxylase synthetase might be hot-spots in Chinese children with holocarboxylase synthetas deficiency. | [Diagnosis, treatment and gene mutation analysis in children with holocarboxylase synthetas deficiency].
Wang T, Ye J, Han LS, Qiu WJ, Zhang HW, Zhang YF, Gao XL, Wang Y, Gu XF. | 04/12/2010 |
| The study shows that not all the proteins and polypeptides that interact with holocarboxylase synthetase are targets for biotinylation, but that carboxylase- and histone-like structures are preferred HCS targets. | The polypeptide Syn67 interacts physically with human holocarboxylase synthetase, but is not a target for biotinylation.
Hassan YI, Moriyama H, Zempleni J., Free PMC Article | 03/22/2010 |
| These results provide insights into substrate recognition by hHCS, which can be distinguished from BirA in this respect. | Substrate recognition characteristics of human holocarboxylase synthetase for biotin ligation.
Lee CK, Cheong C, Jeon YH. | 03/22/2010 |
| 12 patients with multiple carboxylase deficiency, six mutations were found in the BT gene and 4 in the HLCS gene, including 5 novel mutations. | [Gene mutation analyses in Chinese children with multiple carboxylase deficiency].
Wang T, Ye J, Han LS, Qiu WJ, Zhang HW, Zhang YF, Gao XL, Wang Y, Gu XF. | 01/21/2010 |
| Amino termini of HCS influence biotin acceptor substrate recognition | Distinct amino termini of two human HCS isoforms influence biotin acceptor substrate recognition.
Ingaramo M, Beckett D., Free PMC Article | 01/21/2010 |
| The aim of this study was to investigate the effects of holocarboxylase synthetase (HCS) gene to irradiation in a time- and dose-dependent manner. | Gamma-ray up-regulated holocarboxylase synthetase gene.
Ding K, Yang C, Shen J, Xu L, Li Y, Zhou P, Zeng Y. | 01/21/2010 |
| The hypothesis that N- and C-termini play roles in substrate recognition by HCS, was tested. | N- and C-terminal domains in human holocarboxylase synthetase participate in substrate recognition.
Hassan YI, Moriyama H, Olsen LJ, Bi X, Zempleni J., Free PMC Article | 01/21/2010 |
| findings from this study are consistent with the theory that HCS senses biotin, and that biotin regulates its own cellular uptake by participating in HCS-dependent chromatin remodeling events at the SMVT promoter 1 locus in Jurkat cells. | Holocarboxylase synthetase regulates expression of biotin transporters by chromatin remodeling events at the SMVT locus.
Gralla M, Camporeale G, Zempleni J., Free PMC Article | 01/21/2010 |
| Study investigated cell lines from 2 HLCS-deficient patients p.L216R allele; enzyme activity was decreased for p.L216R and could not be increased by additional biotin; furthermore, the turn-over rate for the mutant protein was double that of wildtype. | Reduced half-life of holocarboxylase synthetase from patients with severe multiple carboxylase deficiency.
Bailey LM, Ivanov RA, Jitrapakdee S, Wilson CJ, Wallace JC, Polyak SW. | 01/21/2010 |