Work

Structural and biochemical analyses of a novel bacterial dual specificity phosphatase from Candidatus Chlorohelix allophototropha

Year: 2026

Type: article

Abstract: Dual specificity phosphatases (DUSPs) are a subfamily of protein tyrosine phosphatases that regulate diverse cellular processes through dephosphorylation of phosphorylated substrates. DUSPs are commonly found in eukaryotes, bacteria, archaea, and viruses. However, structural and biochemical characterization of bacterial DUSP remains limited, as only one bacterial DUSP has been identified thus far. In this study, we investigated a novel putative bacterial DUSP from Candidatus Chlorohelix allophototropha, referred to as CCaDUSP. The crystal structure of CCaDUSP showed the presence of a well-conserved catalytic motif with a characteristic phosphate-binding loop. Biochemical analyses further confirmed that CCaDUSP exhibits phosphatase activity and contains dual general acid/base residues, both of which contribute to its enzymatic activity. These findings not only represent the first characterization of a novel bacterial DUSP with dual general acid/base residues but also provide a foundation for understanding the diversity of DUSP proteins in bacteria.

Source: The Journal of Microbiology

DOI: 10.71150/jm.2604025

Authors: Sujin Jung, So Hyeon Park, Joon Sig Choi, Ho-Chul Shin, Seung Jun Kim, Bonsu Ku

Institutions: Chungnam National University, Korea Research Institute of Bioscience and Biotechnology

Language: English

Topic: Protein Tyrosine Phosphatases

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,690

Funders: National Research Foundation, Korea Research Institute of Bioscience and Biotechnology, National Research Foundation of Korea, National Research Council of Science and Technology