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Updated: Jun 6, 2025

Purification of a High Molecular Mass Protein in Streptococcus mutans
Published on: September 14, 2019
The reduced interaction between SufS and SufU in Mycoplasma penetrans results in diminished sulfotransferase activity
Danyang Ma1, Hui Yao1, Yuhua Liu1
1Key Laboratory of Chemical Biology and Molecular Engineering of Education Ministry, Key Laboratory of Energy Conversion and Storage Materials of Shanxi Provence, Institute of Molecular Science, Shanxi University, Taiyuan 030006, China.
Abstract:
Mycoplasma Penetrans (Mpe) is an AIDS-related mycoplasma that is also closely related to respiratory diseases. Proteins involved in the first phase of Fe-S cluster biosynthesis in the SUF-like pathway are essential in Gram-positive bacteria because there is no redundant Fe-S cluster biosynthetic pathway in these proteins. In this study, we characterized two essential proteins: cysteine desulphurase (MpeSufS) and sulfurtransferase (MpeSufU) in Mpe, and resolved their crystal structures. Our results reveal that MpeSufS belongs to type II cysteine desulfurase, and MpeSufU is a Zn2+-containing sulfurtransferase. Residue Q342 in MpeSufS and the zinc atom in MpeSufU mediate sulfur transfer from MpeSufS to MpeSufU. Mutation of Q342 significantly impacts the cysteine desulfurase activity. This study provides new insights into the regulation of the activity of the SufS-SufU complex, which will help guide the design of drugs for the treatment of mycoplasma infections.
Insights
Researchers studied essential proteins MpeSufS and MpeSufU in Mycoplasma Penetrans, revealing how they transfer sulfur for iron-sulfur cluster biosynthesis. This finding aids in developing new treatments for mycoplasma infections.
Area of Science:
- Microbiology
- Structural Biology
- Biochemistry
Background:
- Mycoplasma Penetrans (Mpe) is linked to AIDS and respiratory illnesses.
- Iron-sulfur (Fe-S) cluster biosynthesis via the SUF-like pathway is critical in Gram-positive bacteria due to the absence of redundant pathways.
Purpose of the Study:
- To characterize two essential proteins, cysteine desulfurase (MpeSufS) and sulfurtransferase (MpeSufU), involved in Fe-S cluster biosynthesis in Mpe.
- To resolve the crystal structures of MpeSufS and MpeSufU.
- To elucidate the mechanism of sulfur transfer between these proteins.
Main Methods:
- Protein characterization of MpeSufS and MpeSufU.
- X-ray crystallography to determine the structures of MpeSufS and MpeSufU.
- Site-directed mutagenesis to investigate the role of specific residues and metal ions.
Main Results:
- MpeSufS was identified as a type II cysteine desulfurase.
- MpeSufU was characterized as a zinc (Zn2+)-containing sulfurtransferase.
- Residue Q342 in MpeSufS and the zinc atom in MpeSufU were found to mediate sulfur transfer.
- Mutation of Q342 significantly impaired cysteine desulfurase activity.
Conclusions:
- The study provides structural and mechanistic insights into the SufS-SufU complex in Mycoplasma Penetrans.
- Understanding the regulation of sulfur transfer is crucial for targeting Fe-S cluster biosynthesis.
- These findings can inform the development of novel therapeutic strategies against Mpe infections.
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