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Limited proteolysis for PTM analysis

ABSTRACT: PTMs on a mycobacterial DNA-binding protein with a long, lysine-rich, intrinsically disorders region were analyzed by limited proteolysis with trypsin, unveiling a massive methylation of most lysine residues of the protein in quantitative manner, which was lacked in the recombinant version of the protein expressed in E. coli.

ORGANISM(S): Escherichia Coli Mycobacterium Tuberculosis Mycolicibacterium Smegmatis Mc2 155

SUBMITTER: Sohkichi Matsumoto

PROVIDER: PXD042969 | JPOST Repository | Fri Jun 14 00:00:00 BST 2024

REPOSITORIES: jPOST

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			Action	DRS
	TT5600_20210526_M-BA-YO-001%2312.mgf	Mgf
	TT5600_20210526_M-BA-YO-001%2313.mgf	Mgf
	TT5600_20210526_M-BA-YO-001%2314.mgf	Mgf
	TT5600_20210526_M-BA-YO-001%2315.mgf	Mgf
	TT5600_20210526_M-BA-YO-001%2316.mgf	Mgf

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Publications

Limited proteolysis of mycobacterial DNA-binding protein 1 with an extended, lysine-rich, intrinsically disordered region to unveil posttranslational modifications.

Yoshida Yutaka Y Nishiyama Akihito A Suameitria Dewi Desak Nyoman Surya DNS Yamazaki Tomoya T Yokoyama Akira A Kobayashi Daiki D Kondo Hitoshi H Ozeki Yuriko Y Matsumoto Sohkichi S

Biochemical and biophysical research communications 20230920

The basic, intrinsically disordered regions of eukaryotic histones and their bacterial counterparts are presumed to act as signaling hubs to regulate the compaction of chromosomes or nucleoids and various DNA processes such as gene expression, recombination, and DNA replication. Posttranslational modifications (PTMs) on these regions are pivotal in regulating chromosomal or nucleoid compaction and DNA processes. However, the low sequence complexity and the presence of short lysine-rich repeats i ...[more]

PMID: 37774568

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Project description:Yin Yang 1 (YY1) is a multifunctional transcription factor shown to be critical in a variety of biological processes. Although it has been reported to be regulated by multiple types of post-translational modifications (PTMs), whether YY1 is methylated, which enzyme methylates YY1, and hence the functional significance of YY1 methylation remain completely unknown. Here we reported the first methyltransferase, SET7/9 (KMT7), capable of methylating YY1 in vitro and in vivo at two highly conserved lysine (K) residues, K173 and K411, located in two distinct domains, one in the central glycine-rich region and the other in the very carboxyl-terminus. Functional study revealed that SET7/9-mediated YY1 methylation regulated YY1 DNA-binding activity both in vitro and at specific genomic loci in cultured cells. Consistently, SET7/9-mediated YY1 methylation was shown to involve in YY1-regulated gene transcription and cell proliferation. Our findings revealed a novel regulatory strategy, methylation by lysine methyltransferase, imposed on YY1 protein, and linked YY1 methylation with its biological functions.

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Structures of RNA polymerase II complexes with Bye1, a chromatin-binding PHF3/DIDO homologue

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