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Nucleotide sequence of the protein D2 gene of Pseudomonas aeruginosa
H Yoneyama1, E Yoshihara, T Nakae
1Department of Molecular Life Science, Tokai University School of Medicine, Isehara, Japan.
Abstract:
Protein D2 of the outer membrane of Pseudomonas aeruginosa was shown to form the imipenem-permeable pore. We cloned and sequenced the protein D2 gene. The protein D2 gene encodes a polypeptide with 443 amino acids consisting of 23 and 420 amino acid residues for the signal peptide and mature polypeptide (M(r), 46,010), respectively. Protein D2 contains the highest molar ratio of glycine and no cysteine. The polar amino acids are scattered throughout the sequence.
Insights
Pseudomonas aeruginosa outer membrane protein D2 forms the imipenem-permeable pore. Its gene was sequenced, revealing a 443-amino acid polypeptide structure crucial for antibiotic diffusion.
Area of Science:
- Microbiology
- Structural Biology
- Genetics
Background:
- Pseudomonas aeruginosa is an opportunistic pathogen known for its intrinsic resistance to antibiotics.
- Outer membrane proteins (OMPs) play a critical role in the permeability barrier of Gram-negative bacteria.
- Understanding the function of specific OMPs is essential for developing strategies to overcome antibiotic resistance.
Purpose of the Study:
- To characterize Protein D2 from Pseudomonas aeruginosa.
- To determine the role of Protein D2 in imipenem permeability.
- To elucidate the genetic and structural features of Protein D2.
Main Methods:
- Cloning and sequencing of the protein D2 gene.
- Bioinformatic analysis of the deduced amino acid sequence.
- Functional characterization of Protein D2 in relation to imipenem transport.
Main Results:
- Protein D2 was identified as the imipenem-permeable pore in the Pseudomonas aeruginosa outer membrane.
- The protein D2 gene encodes a 443-amino acid polypeptide, including a signal peptide and a mature protein of 420 amino acids (M(r) 46,010).
- Protein D2 exhibits a high molar ratio of glycine and lacks cysteine residues, with polar amino acids distributed throughout its sequence.
Conclusions:
- Protein D2 functions as a key porin facilitating imipenem diffusion across the outer membrane of Pseudomonas aeruginosa.
- The structural characteristics of Protein D2, such as its amino acid composition, may influence its pore-forming properties.
- Further investigation into Protein D2 could provide insights into antibiotic resistance mechanisms and potential therapeutic targets.