Work

Identification of the YEATS domain of GAS41 as a pH-dependent reader of histone succinylation

Year: 2018

Type: article

Abstract: Significance Posttranslational modifications (PTMs) on histone lysines regulate gene expression and physiological functions. Succinylation is a newly discovered PTM with distinctive features. However, rarely studies have shown the function of succinylation on histone lysines. Our biochemical and structural studies demonstrate that GAS41, an oncogene-coded protein, can act as the reader of succinylation on histone H3K122. The functional significance of the pH-dependent histidine of GAS41 recognizing succinyl lysine (Ksuc) could have implications in local pH-dysregulated circumstances. The mechanism illustrated by the structures also provides an important insight into the development of specific regulators targeting the GAS41 YEATS domain in the future.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.1717664115

Authors: Yi Wang, Jing Jin, Matthew Wai Heng Chung, Ling Feng, Hongyan Sun, Quan Hao

Institutions: University of Hong Kong, City University of Hong Kong, City University of Hong Kong, Shenzhen Research Institute

Language: English

Topic: Genomics and Chromatin Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funders: National Natural Science Foundation of China, Research Grants Council, University Grants Committee

Awards: G2596906936, 多肽芯片应用于高通量研究溴结构域和去乙酰化酶, G6243181997, G942926612