Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Mumbai 400076, India.
Biochemistry. 2013 Jan 15;52(2):392-401. doi: 10.1021/bi301237m. Epub 2012 Dec 28.
MciZ, a peptide with 40 amino acid residues, has been shown to be expressed during bacterial sporulation, to inhibit Z-ring formation in bacteria, and to inhibit the assembly of FtsZ in vitro. Here, MciZ was found to bind to FtsZ in vitro with a dissociation constant of 0.3 ± 0.1 μM. Guanosine nucleotides inhibited the binding of MciZ to FtsZ; however, GTP inhibited the binding of MciZ to FtsZ more strongly than GDP. In addition, MciZ inhibited the binding of 2',3'-O-(2,4,6-trinitrocyclohexadienylidene)-GTP, a fluorescent analogue of GTP, to FtsZ. The results indicated that MciZ shares its binding site on FtsZ with GTP. Furthermore, M19I, an N-terminal 19-residue peptide (MKVHRMPKGVVLVGKAWEI) of MciZ, inhibited the assembly and GTPase activity of FtsZ in vitro. The results suggested that GTP plays an important role in the regulation of the interaction between FtsZ and MciZ and that M19I may be used as a lead peptide to design peptide inhibitors of FtsZ assembly.
MciZ 是一种含有 40 个氨基酸残基的肽,已被证明在细菌孢子形成过程中表达,抑制细菌 Z 环的形成,并抑制 FtsZ 在体外的组装。在这里,发现 MciZ 以 0.3±0.1μM 的解离常数在体外与 FtsZ 结合。鸟苷核苷酸抑制 MciZ 与 FtsZ 的结合;然而,GTP 比 GDP 更强烈地抑制 MciZ 与 FtsZ 的结合。此外,MciZ 抑制了 2',3'-O-(2,4,6-三硝基环己二烯亚基)-GTP(GTP 的荧光类似物)与 FtsZ 的结合。结果表明,MciZ 与 GTP 共享其在 FtsZ 上的结合位点。此外,MciZ 的 N 端 19 个残基肽(MKVHRMPKGVVLVGKAWEI)M19I 在体外抑制 FtsZ 的组装和 GTPase 活性。结果表明,GTP 在调节 FtsZ 和 MciZ 之间的相互作用中起重要作用,并且 M19I 可用作设计 FtsZ 组装肽抑制剂的先导肽。