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"Identification of Novel Zinc-Dependent Peptidases: Characterization of MEP3, MEP4, MCPA, and MCPB cDNA Clones."
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"Identification of Novel Zinc-Dependent Peptidases: Characterization of MEP3, MEP4, MCPA, and MCPB cDNA Clones."This study involves both endopeptidases (MEP) and exopeptidases (MCP), the abstract should emphasize the discovery of a complete proteolytic toolkit within Trichophyton rubrum and Trichophyton mentagrophytes.AbstractBackground: Metallopeptidases play indispensable roles in protein catabolism, signaling peptide processing, and physiological regulation. Among these, the M3/M4 families (MEP) and M14 family (MCP) are critical for both internal peptide cleavage and C-terminal processing. Despite their importance, the molecular identities of these enzymes in Trichophyton rubrum and Trichophyton mentagrophytes have remained largely uncharacterized.Objectives: The aim of this study was to identify, clone, and bioinformatically characterize the full-length complementary DNAs (cDNAs) for Metalloprotease 3 and 4 (MEP3, MEP4) and Metallocarboxypeptidase A and B (MCP A, MCP B) using an Expressed Sequence Tag (EST) database approach.Methodology: Candidate sequences were identified from an EST library through in silico screening using conserved MEROPS peptidase domains. Following lead identification, the complete open reading frames (ORFs) were amplified via RT-PCR. Sequence analysis was performed to predict conserved motifs, signal peptides, and phylogenetic relationships.Results: We successfully cloned four distinct cDNAs. Sequence analysis revealed the presence of the signature zinc-binding motif in MEP3 and MEP4, while MCP A and B exhibited the characteristic active site residues of the M14 carboxypeptidase family. Bioinformatic modeling predicted that MEP3/4 are likely [e.g., secreted/cytosolic] enzymes, while the MCPs contain a pro-domain consistent with zymogen activation. Phylogenetic analysis clustered these sequences with known orthologs in Trichophyton rubrum and Trichophyton mentagrophytes., suggesting high evolutionary conservation of the proteolytic machinery.Conclusion: The cloning of these four peptidases provides the first molecular evidence of a coordinated metallopeptidase system in Trichophyton rubrum and Trichophyton mentagrophytes.
Title: "Identification of Novel Zinc-Dependent Peptidases: Characterization of MEP3, MEP4, MCPA, and MCPB cDNA Clones."
Description:
"Identification of Novel Zinc-Dependent Peptidases: Characterization of MEP3, MEP4, MCPA, and MCPB cDNA Clones.
"This study involves both endopeptidases (MEP) and exopeptidases (MCP), the abstract should emphasize the discovery of a complete proteolytic toolkit within Trichophyton rubrum and Trichophyton mentagrophytes.
AbstractBackground: Metallopeptidases play indispensable roles in protein catabolism, signaling peptide processing, and physiological regulation.
Among these, the M3/M4 families (MEP) and M14 family (MCP) are critical for both internal peptide cleavage and C-terminal processing.
Despite their importance, the molecular identities of these enzymes in Trichophyton rubrum and Trichophyton mentagrophytes have remained largely uncharacterized.
Objectives: The aim of this study was to identify, clone, and bioinformatically characterize the full-length complementary DNAs (cDNAs) for Metalloprotease 3 and 4 (MEP3, MEP4) and Metallocarboxypeptidase A and B (MCP A, MCP B) using an Expressed Sequence Tag (EST) database approach.
Methodology: Candidate sequences were identified from an EST library through in silico screening using conserved MEROPS peptidase domains.
Following lead identification, the complete open reading frames (ORFs) were amplified via RT-PCR.
Sequence analysis was performed to predict conserved motifs, signal peptides, and phylogenetic relationships.
Results: We successfully cloned four distinct cDNAs.
Sequence analysis revealed the presence of the signature zinc-binding motif in MEP3 and MEP4, while MCP A and B exhibited the characteristic active site residues of the M14 carboxypeptidase family.
Bioinformatic modeling predicted that MEP3/4 are likely [e.
g.
, secreted/cytosolic] enzymes, while the MCPs contain a pro-domain consistent with zymogen activation.
Phylogenetic analysis clustered these sequences with known orthologs in Trichophyton rubrum and Trichophyton mentagrophytes.
, suggesting high evolutionary conservation of the proteolytic machinery.
Conclusion: The cloning of these four peptidases provides the first molecular evidence of a coordinated metallopeptidase system in Trichophyton rubrum and Trichophyton mentagrophytes.