In vitro polymerization of Mycobacterium leprae FtsZ OR Mycobacterium tuberculosis FtsZ is revived or abolished, respectively, by reciprocal mutation of a single residue.
A single residue that dramatically influences polymerization of principal cell division protein FtsZ of Mycobacterium leprae (MlFtsZ) and Mycobacterium tuberculosis (MtFtsZ) has been identified. Soluble, recombinant MlFtsZ did not show polymerization in vitro, in contrast to MtFtsZ, which polymerised. Mutation of the lone non-conserved residue T172 in the N-terminal domain of MlFtsZ to A172, as it exists in MtFtsZ, showed dramatic polymerization of MlFtsZ-T172A in vitro. Reciprocal mutation of A172 in MtFtsZ to T172, as it exists in MlFtsZ, abolished polymerization of MtFtsZ-A172T in vitro. While T172A mutation enhanced weak GTPase activity of MlFtsZ, reciprocal A172T mutation marginally reduced GTPase activity of MtFtsZ in vitro. These observations demonstrate that the residue at position 172 plays critical role in the polymerization of MlFtsZ and MtFtsZ. A possible evolutionary correlation between the presence of polymerization-adversive or polymerization-favouring residue at position 172 in FtsZ and generation time of the respective bacterium are discussed.
Gupta
Prabuddha
P
Department of Microbiology and Cell Biology, Indian Institute of Science, Malleshwaram, Bangalore, Karnataka 560012, India.
Srinivasan
Ramanujam
R
Rajeswari
Haryadi
H
Indi
Shantinath
S
Ajitkumar
Parthasarathi
P
D001426:Bacterial Proteins / Q000737:chemistry*; D001665:Binding Sites; D003598:Cytoskeletal Proteins / Q000737:chemistry*; D019281:Dimerization; D016297:Mutagenesis, Site-Directed; D009166:Mycobacterium leprae / Q000737:chemistry*; D009169:Mycobacterium tuberculosis / Q000737:chemistry*; D011485:Protein Binding; D013045:Species Specificity; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; C071525:FtsZ protein, Bacteria