MecA: A Multifunctional ClpP-Dependent and Independent Regulator in Gram-Positive Bacteria
Document Type
Article
Publication Date
3-11-2025
Publication Title
Molecular Microbiology
Abstract
MecA is a broadly conserved adaptor protein in Gram-positive bacteria, mediating the recognition and degradation of specific target proteins by ClpCP protease complexes. MecA binds target proteins, often through recognition of degradation tags or motifs, and delivers them to the ClpC ATPase, which unfolds and translocates the substrates into the ClpP protease barrel for degradation. MecA activity is tightly regulated through interactions with ClpC ATPase and other factors, ensuring precise control over protein degradation and cellular homeostasis. Beyond proteolysis, emerging evidence highlights a ClpP-independent role of MecA in modulating the function of its targets, including key enzymes and transcriptional factors involved in biosynthetic and metabolic pathways. However, the full scope and mechanisms of ClpP-independent MecA regulation remain unclear, warranting further investigation.
PubMed ID
40070161
Recommended Citation
Wen, Zezhang T.; Ellepola, Kassapa; and Wu, Hui, "MecA: A Multifunctional ClpP-Dependent and Independent Regulator in Gram-Positive Bacteria" (2025). School of Dentistry Faculty Publications. 186.
https://digitalscholar.lsuhsc.edu/sod_facpubs/186
10.1111/mmi.15356