相似文献

1

Prokaryotic BirA ligase biotinylates K4, K9, K18 and K23 in histone H3.

BMB Rep. 2008 Apr 30;41(4):310-5. doi: 10.5483/bmbrep.2008.41.4.310.

2

Holocarboxylase synthetase is a chromatin protein and interacts directly with histone H3 to mediate biotinylation of K9 and K18.

J Nutr Biochem. 2011 May;22(5):470-5. doi: 10.1016/j.jnutbio.2010.04.001. Epub 2010 Aug 5.

3

K4, K9 and K18 in human histone H3 are targets for biotinylation by biotinidase.

FEBS J. 2005 Aug;272(16):4249-59. doi: 10.1111/j.1742-4658.2005.04839.x.

4

Nonenzymatic biotinylation of histone H2A.

Protein Sci. 2009 Feb;18(2):314-28. doi: 10.1002/pro.37.

5

Lysine residues in N-terminal and C-terminal regions of human histone H2A are targets for biotinylation by biotinidase.

J Nutr Biochem. 2006 Apr;17(4):225-33. doi: 10.1016/j.jnutbio.2005.05.003. Epub 2005 Jun 8.

6

Expression and purification of E. coli BirA biotin ligase for in vitro biotinylation.

Protein Expr Purif. 2012 Mar;82(1):162-7. doi: 10.1016/j.pep.2011.12.008. Epub 2012 Jan 2.

7

A bacterial display system for effective selection of protein-biotin ligase BirA variants with novel peptide specificity.

Sci Rep. 2019 Mar 11;9(1):4118. doi: 10.1038/s41598-019-40984-x.

8

Promiscuous protein biotinylation by Escherichia coli biotin protein ligase.

Protein Sci. 2004 Nov;13(11):3043-50. doi: 10.1110/ps.04911804. Epub 2004 Sep 30.

9

Holocarboxylase synthetase interacts physically with euchromatic histone-lysine N-methyltransferase, linking histone biotinylation with methylation events.

J Nutr Biochem. 2013 Aug;24(8):1446-52. doi: 10.1016/j.jnutbio.2012.12.003. Epub 2013 Jan 20.

10

Elucidating combinatorial histone modifications and crosstalks by coupling histone-modifying enzyme with biotin ligase activity.

Nucleic Acids Res. 2013 Feb 1;41(3):e49. doi: 10.1093/nar/gks1247. Epub 2012 Dec 20.

引用本文的文献

1

Resveratrol compounds inhibit human holocarboxylase synthetase and cause a lean phenotype in Drosophila melanogaster.

J Nutr Biochem. 2015 Nov;26(11):1379-84. doi: 10.1016/j.jnutbio.2015.07.004. Epub 2015 Jul 26.

2

A comprehensive view of the epigenetic landscape. Part II: Histone post-translational modification, nucleosome level, and chromatin regulation by ncRNAs.

Neurotox Res. 2015 Feb;27(2):172-97. doi: 10.1007/s12640-014-9508-6. Epub 2014 Dec 17.

3

β-Keto and β-hydroxyphosphonate analogs of biotin-5'-AMP are inhibitors of holocarboxylase synthetase.

Bioorg Med Chem Lett. 2014 Dec 15;24(24):5568-5571. doi: 10.1016/j.bmcl.2014.11.010. Epub 2014 Nov 7.

4

Holocarboxylase synthetase interacts physically with nuclear receptor co-repressor, histone deacetylase 1 and a novel splicing variant of histone deacetylase 1 to repress repeats.

Biochem J. 2014 Aug 1;461(3):477-86. doi: 10.1042/BJ20131208.

5

Epigenomic programing: a future way to health?

Microb Ecol Health Dis. 2014 May 8;25. doi: 10.3402/mehd.v25.24145. eCollection 2014.

6

Novel roles of holocarboxylase synthetase in gene regulation and intermediary metabolism.

Nutr Rev. 2014 Jun;72(6):369-76. doi: 10.1111/nure.12103. Epub 2014 Mar 28.

7

Holocarboxylase synthetase 1 physically interacts with histone h3 in Arabidopsis.

Scientifica (Cairo). 2013;2013:983501. doi: 10.1155/2013/983501. Epub 2013 Feb 12.

8

Holocarboxylase synthetase catalyzes biotinylation of heat shock protein 72, thereby inducing RANTES expression in HEK-293 cells.

Am J Physiol Cell Physiol. 2013 Dec 15;305(12):C1240-5. doi: 10.1152/ajpcell.00279.2013. Epub 2013 Oct 16.

9

Gut indigenous microbiota and epigenetics.

Microb Ecol Health Dis. 2012 Mar 28;23. doi: 10.3402/mehd.v23i0.17195. eCollection 2012.

10

Biotinylation of lysine 16 in histone H4 contributes toward nucleosome condensation.

Arch Biochem Biophys. 2013 Jan 15;529(2):105-11. doi: 10.1016/j.abb.2012.11.005. Epub 2012 Dec 5.

本文引用的文献

1

Artifactual detection of biotin on histones by streptavidin.

Anal Biochem. 2008 Feb 1;373(1):71-7. doi: 10.1016/j.ab.2007.09.003. Epub 2007 Sep 8.

2

Holocarboxylase synthetase regulates expression of biotin transporters by chromatin remodeling events at the SMVT locus.

J Nutr Biochem. 2008 Jun;19(6):400-8. doi: 10.1016/j.jnutbio.2007.06.002. Epub 2007 Sep 27.

3

K12-biotinylated histone H4 marks heterochromatin in human lymphoblastoma cells.

J Nutr Biochem. 2007 Nov;18(11):760-8. doi: 10.1016/j.jnutbio.2006.12.014. Epub 2007 Apr 16.

4

Susceptibility to heat stress and aberrant gene expression patterns in holocarboxylase synthetase-deficient Drosophila melanogaster are caused by decreased biotinylation of histones, not of carboxylases.

J Nutr. 2007 Apr;137(4):885-9. doi: 10.1093/jn/137.4.885.

5

Drosophila melanogaster holocarboxylase synthetase is a chromosomal protein required for normal histone biotinylation, gene transcription patterns, lifespan, and heat tolerance.

J Nutr. 2006 Nov;136(11):2735-42. doi: 10.1093/jn/136.11.2735.

6

Mutations in the holocarboxylase synthetase gene HLCS.

Hum Mutat. 2005 Oct;26(4):285-90. doi: 10.1002/humu.20204.

7

Lysine residues in N-terminal and C-terminal regions of human histone H2A are targets for biotinylation by biotinidase.

J Nutr Biochem. 2006 Apr;17(4):225-33. doi: 10.1016/j.jnutbio.2005.05.003. Epub 2005 Jun 8.

8

K4, K9 and K18 in human histone H3 are targets for biotinylation by biotinidase.

FEBS J. 2005 Aug;272(16):4249-59. doi: 10.1111/j.1742-4658.2005.04839.x.

9

K8 and K12 are biotinylated in human histone H4.

Eur J Biochem. 2004 Jun;271(11):2257-63. doi: 10.1111/j.1432-1033.2004.04167.x.

10

Reduced histone biotinylation in multiple carboxylase deficiency patients: a nuclear role for holocarboxylase synthetase.

Hum Mol Genet. 2004 Jan 1;13(1):15-23. doi: 10.1093/hmg/ddh006. Epub 2003 Nov 12.

文献AI研究员

20分钟写一篇综述，助力文献阅读效率提升50倍。

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

文档翻译

学术文献翻译模型，支持多种主流文档格式。

原核生物BirA连接酶可将生物素连接到组蛋白H3的K4、K9、K18和K23位点上。

Prokaryotic BirA ligase biotinylates K4, K9, K18 and K23 in histone H3.

作者信息

Kobza Keyna, Sarath Gautam, Zempleni Janos

机构信息

Departments of Nutrition and Health Sciences, University of Nebraska at Lincoln, Lincoln, NE, USA.

出版信息

BMB Rep. 2008 Apr 30;41(4):310-5. doi: 10.5483/bmbrep.2008.41.4.310.

DOI:10.5483/bmbrep.2008.41.4.310

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2377390/

Abstract

BirA ligase is a prokaryotic ortholog of holocarboxylase synthetase (HCS) that can biotinylate proteins. This study tested the hypothesis that BirA ligase catalyzes the biotinylation of eukaryotic histones. If so, this would mean that recombinant BirA ligase is a useful surrogate for HCS in studies of histone biotinylation. The biological activity of recombinant BirA ligase was confirmed by enzymatic biotinylation of p67. In particular, it was found that BirA ligase biotinylated both calf thymus histone H1 and human bulk histone extracts. Incubation of recombinant BirA ligase with H3-based synthetic peptides showed that lysines 4, 9, 18, and 23 in histone H3 are the targets for the biotinylation by BirA ligase. Modification of the peptides (e.g., serine phosphorylation) affected the subsequent biotinylation by BirA ligase, suggesting crosstalk between modifications. In conclusion, this study suggests that prokaryotic BirA ligase is a promiscuous enzyme and biotinylates eukaryotic histones. Moreover the biotinylation of histones by BirA ligase is consistent with the proposed role of human HCS in chromatin.

摘要

BirA连接酶是全羧化酶合成酶（HCS）的原核直系同源物，能够对蛋白质进行生物素化修饰。本研究检验了BirA连接酶催化真核生物组蛋白生物素化修饰的假说。如果真是这样，这将意味着在组蛋白生物素化修饰研究中，重组BirA连接酶是HCS的一种有用替代物。通过对p67进行酶促生物素化修饰，证实了重组BirA连接酶的生物活性。具体而言，发现BirA连接酶可对小牛胸腺组蛋白H1和人总组蛋白提取物进行生物素化修饰。重组BirA连接酶与基于H3的合成肽一起孵育表明，组蛋白H3中的赖氨酸4、9、18和23是BirA连接酶进行生物素化修饰的靶点。对肽进行修饰（例如丝氨酸磷酸化）会影响随后BirA连接酶的生物素化修饰，这表明修饰之间存在相互作用。总之，本研究表明原核生物BirA连接酶是一种通用性酶，可对真核生物组蛋白进行生物素化修饰。此外，BirA连接酶对组蛋白的生物素化修饰与人类HCS在染色质中所起的作用一致。