Recombinant Candida albicans Presequence translocated-associated motor subunit PAM17, mitochondrial (PAM17)

Introduction to Recombinant Candida albicans Presequence Translocated-Associated Motor Subunit PAM17, Mitochondrial (PAM17)

Recombinant Candida albicans Presequence Translocated-Associated Motor Subunit PAM17, mitochondrial (PAM17), is a protein involved in the mitochondrial protein import process. While specific research on the recombinant form of PAM17 from Candida albicans is limited, understanding its role in mitochondrial protein import can be inferred from studies on its homologs in other organisms, particularly in yeast like Saccharomyces cerevisiae.

PAM17 is part of the Presequence Translocase-Associated Motor (PAM) complex, which plays a crucial role in the translocation of proteins across the mitochondrial inner membrane. The PAM complex includes several subunits, such as mtHsp70, Pam16, Pam18, and Tim44, each contributing to the efficient import of proteins into the mitochondrial matrix.

Function of PAM17 in Mitochondrial Protein Import

PAM17 is involved in an early stage of protein translocation into the mitochondria. It interacts with the Tim23 presequence translocase, which forms a channel for protein import across the inner mitochondrial membrane . The interaction between PAM17 and Tim23 is crucial for the efficient import of preproteins into the mitochondrial matrix.

Interaction with Other PAM Complex Subunits

PAM17 interacts with other components of the PAM complex, including Tim44 and the J-protein complex (Pam16-Pam18). While Tim44 is essential for recruiting mtHsp70 to the translocase and facilitating later stages of protein import, PAM17's role is more nuanced. In the absence of functional Tim44, PAM17's association with the Tim23 complex increases, suggesting a compensatory mechanism .

3.1. Impact of Tim44 on PAM17 Association

The alteration of Tim44 function leads to a dual effect on the PAM complex: it diminishes the association of the J-complex (Pam16-Pam18) with the Tim23 translocase while enhancing the binding of PAM17 to Tim23. This indicates that PAM17 and the J-complex interact with the Tim23 complex through different sites and are regulated differently by Tim44 .

Research Findings and Implications

Research on PAM17 highlights its role in posttranslational protein import into mitochondria. The deletion of PAM17 in yeast results in an import defect for certain matrix-targeted precursors, although cells generally grow normally under most conditions . This suggests that while PAM17 is not essential for viability, it contributes to the efficiency of protein import.

References - Pam17 and Tim44 act sequentially in protein import into the mitochondria. - Mitochondrial Protein Import Motor: Differential Role of Tim44 in the Recruitment of Pam17 and J-Complex to the Presequence Translocase. - Presequence translocase-associated motor subunits of mitochondria. - Mitochondrial Protein Import Motor: Differential Role of Tim44 in the Recruitment of Pam17 and J-Complex to the Presequence Translocase.