METHOD FOR DETECTING GLYCOSYLATION OF HISTONE PROTEIN, AND ANTIBODY TO BE USED FOR THE SAME

• Main Authors: KATO SHIGEAKI, FUJIKI RYOJI
• Format: Patent
• Language: English
• Published: 26.04.2012
• Subjects: BEER; BIOCHEMISTRY; CHEMISTRY; COMPOSITIONS THEREOF; CULTURE MEDIA; ENZYMOLOGY; FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIREDCHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERSFROM A RACEMIC MIXTURE; INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIRCHEMICAL OR PHYSICAL PROPERTIES; MEASURING; METALLURGY; MICROBIOLOGY; MICROORGANISMS OR ENZYMES; MUTATION OR GENETIC ENGINEERING; ORGANIC CHEMISTRY; PEPTIDES; PHYSICS; PROPAGATING, PRESERVING OR MAINTAINING MICROORGANISMS; SPIRITS; TESTING; VINEGAR; WINE

PROBLEM TO BE SOLVED: To provide a method enabling glycosylation of histone protein to be detected and an antibody to be used for the method.SOLUTION: It is found that histones (histone H2B, histone H2A, histone H3, histone H4) are glycosylated (O-GlcNAcylated) in a nucleus, more particularly, in histone H2B, sites to be GlcNAcylated are the 91st serine residue, the 112th serine residue, and the 123rd serine residue. Additionally, an antibody which binds to a glycosylated site of histone H2B was made and further analyses were performed. Consequently, it is also found that the glycosylation depends on extracellular glucose concentration via HBP, and the enhancement of the glycosylation induces the ubiquitination of histone H2B and the methylation of histone H3, as well as activates the transcription of PGK1 genes or the like.