Identification of a purC gene from Streptococcus pneumoniae
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Updated: Nov 7, 2026
Constructing Mutants in Serotype 1 Streptococcus pneumoniae strain 519/43
Published on: September 11, 2020
1Department of Biological Sciences, University of Illinois at Chicago 60680.
Abstract:
A gene encoding 5'-phosphoribosyl-5-aminoimidazole-4-N-succinocarboxamide synthetase was identified in Streptococcus pneumoniae as a 708-bp segment of the genome encoding a 27,001-Da protein with strong similarity to known PurC proteins. The S. pneumoniae purC gene, found immediately adjacent to the competence induction genes, comAB, was cloned and sequenced. The predicted protein product of purC displayed substantial (> 40%) identity to the entire sequence of the PurC proteins of Bacillus subtilis and Escherichia coli. Function of the S. pneumoniae gene product was demonstrated by complementation of E. coli purC mutations.
Insights
Streptococcus pneumoniae purC gene was identified and sequenced, encoding a protein similar to known PurC enzymes. Its function was confirmed by complementing E. coli purC mutations, advancing understanding of purine biosynthesis in bacteria.
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- Purine biosynthesis is essential for all life.
- The PurC enzyme catalyzes a key step in de novo purine biosynthesis.
- Understanding bacterial purine metabolism is crucial for developing novel antimicrobial strategies.
Purpose of the Study:
- To identify and characterize the purC gene in Streptococcus pneumoniae.
- To determine the functional role of the S. pneumoniae PurC protein.
- To investigate the evolutionary conservation of the PurC enzyme.
Main Methods:
- Genomic identification and sequencing of the S. pneumoniae purC gene.
- Bioinformatic analysis of the predicted protein sequence.
- Functional complementation of Escherichia coli purC mutants.
Main Results:
- A 708-bp gene encoding 5'-phosphoribosyl-5-aminoimidazole-4-N-succinocarboxamide synthetase (PurC) was identified in S. pneumoniae.
- The S. pneumoniae PurC protein showed >40% sequence identity to homologous proteins from B. subtilis and E. coli.
- Complementation of E. coli purC mutations confirmed the functional activity of the S. pneumoniae gene product.
Conclusions:
- The identified gene in S. pneumoniae encodes a functional PurC enzyme.
- The S. pneumoniae purC gene is conserved among bacterial species.
- This study provides insights into purine metabolism in S. pneumoniae and potential targets for drug development.
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