The Functionality of IbpA from Is Governed by Dynamic Rearrangement of Its Globular-Fibrillar Quaternary Structure.

Small heat shock proteins (sHSPs) represent a first line of stress defense in many bacteria. The primary function of these molecular chaperones involves preventing irreversible protein denaturation and aggregation. In , fibrillar IbpA binds unfolded proteins and keeps them in a folding-competent state.

The division protein FtsZ interacts with the small heat shock protein IbpA in Acholeplasma laidlawii.

Small heat shock proteins (sHSPs) control the proteins stability in the cell preventing their irreversible denaturation. While many mycoplasmas possess the sHSP gene in the genome, Acholeplasma laidlawii is the only mycoplasma capable of surviving in the environment. Here we report that the sHSP IbpA directly interacts with the key division protein FtsZ in A.

N- and C-terminal regions of the small heat shock protein IbpA from competitively govern its oligomerization pattern and chaperone-like activity.

Small heat shock proteins (sHSPs) are ubiquitous molecular chaperones preventing the irreversible denaturation of proteins. While in two sHSPs IbpA and IbpB work in strong cooperation, the sole Mollicute with free-living ability carries a single gene encoding the sHSP protein IbpA. , independently of the temperature, IbpA forms a heterogeneous mixture of approximately 24-mer globules, fibrils and huge protein aggregates.