Dataset Information

LC-MS/MS identification of Kbz sites on histones catalyzed by non-enzymatic and enzymatic ways.

ABSTRACT: Histone lysine benzoylation may occur by Gcn5-catalyzed and nonenzymatically ways in vivo. In this project, we identified several Kbz sites on Xenopus laevis octamer in the absence or presence Gcn5-Ada2 complex in vitro, respectively. The number 672 represents the data in the absence of Gcn5-Ada2, and the number 674 represents the data that in the presence of Gcn5-Ada2.

INSTRUMENT(S): Orbitrap Eclipse

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Duo Wang

LAB HEAD: Chen Yong

PROVIDER: PXD030110 | Pride | 2022-05-19

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

Items per page:

1 - 5 of 5

Publications

Global profiling of regulatory elements in the histone benzoylation pathway.

Wang Duo D Yan Fuxiang F Wu Ping P Ge Kexue K Li Muchun M Li Tingting T Gao Ying Y Peng Chao C Chen Yong Y

Nature communications 20220316 1

Lysine benzoylation (Kbz) is a recently discovered post-translational modification associated with active transcription. However, the proteins for maintaining and interpreting Kbz and the physiological roles of Kbz remain elusive. Here, we systematically characterize writer, eraser, and reader proteins of histone Kbz in S. cerevisiae using proteomic, biochemical, and structural approaches. Our study identifies 27 Kbz sites on yeast histones that can be regulated by cellular metabolic states. The ...[more]

PMID: 35296687

Similar Datasets

Project description:Methylmercury (MeHg) is a potent bioaccumulative neurotoxin that is produced by certain anaerobic bacteria and archaea. Mercury (Hg) methylation has been linked to the gene pair hgcAB, which encodes a membrane-associated corrinoid protein and a ferredoxin. Although microbial Hg methylation has been characterized in vivo, the cellular biochemistry and the specific roles of the gene products HgcA and HgcB in Hg methylation are not well understood. Here, we report the kinetics of Hg methylation in cell lysates of Desulfovibrio desulfuricans ND132 at nanomolar Hg concentrations. The enzymatic Hg methylation mediated by HgcAB is highly oxygen sensitive, irreversible, and follows Michaelis-Menten kinetics, with an apparent Km of 3.2 nM and Vmax of 19.7 fmol · min-1 · mg-1 total protein for the substrate Hg(II). Although the abundance of HgcAB in the cell lysates is extremely low, Hg(II) was quantitatively converted to MeHg at subnanomolar substrate concentrations. Interestingly, increasing thiol/Hg(II) ratios did not impact Hg methylation rates, which suggests that HgcAB-mediated Hg methylation effectively competes with cellular thiols for Hg(II), consistent with the low apparent Km Supplementation of 5-methyltetrahydrofolate or pyruvate did not enhance MeHg production, while both ATP and a nonhydrolyzable ATP analog decreased Hg methylation rates in cell lysates under the experimental conditions. These studies provide insights into the biomolecular processes associated with Hg methylation in anaerobic bacteria.IMPORTANCE The concentration of Hg in the biosphere has increased dramatically over the last century as a result of industrial activities. The microbial conversion of inorganic Hg to MeHg is a global public health concern due to bioaccumulation and biomagnification of MeHg in food webs. Exposure to neurotoxic MeHg through the consumption of fish represents a significant risk to human health and can result in neuropathies and developmental disorders. Anaerobic microbial communities in sediments and periphyton biofilms have been identified as sources of MeHg in aquatic systems, but the associated biomolecular mechanisms are not fully understood. In the present study, we investigate the biochemical mechanisms and kinetics of MeHg formation by HgcAB in sulfate-reducing bacteria. These findings advance our understanding of microbial MeHg production and may help inform strategies to limit the formation of MeHg in the environment.

			Action	DRS
	chenyong672.mgf	Mgf
	chenyong672.raw	Raw
	chenyong674.mgf	Mgf
	chenyong674.raw	Raw
	peptides_1_1_0.mzid.gz	Mzid