![]() In B, data from 3 replicates are presented as mean ± SEM. C-terminal sequences shown belong to the consensus C motif-2 family of ClpX recognition tags (R/H-x-K/R-K-Φ with x representing any amino acid and Φ representing a hydrophobic amino acid residue). Alignment of the C-terminal amino acid sequences of several proteins recognized by ClpX. ![]() Side chains are shown for R379 (red) and K380 (blue). Structural model of the C-terminal alpha-helical region of FtsZ, residues 367 through 383, that cocrystallized with ZipA (PDB entry 1F47). Comparison of rates of degradation of FtsZ wild type and mutant proteins in the presence and absence of GTP from in vitro degradation reactions containing 10 µM wild type or mutant fluorescent FtsZ and 1 µM ClpXP. The C-terminal FtsZ deletions and substitution mutations used here are presented. Linear schematic diagram of FtsZ protein separated into three regions: the polymerization domain (amino acids 1 through 316), the unstructured linker (amino acids 317 through 369) and the C-terminal domain or conserved core region (amino acids 370 through 383). We also observed that in vitro MinC inhibits degradation of FtsZ by ClpXP, suggesting that some of the same residues in the C-terminal site that are important for degradation by ClpXP are important for binding MinC.Ī. Mutation of either region caused the protein to be more stable and mutation of both caused an additive effect, suggesting that both regions are important. ![]() The other region is near the FtsZ C-terminus and partially overlaps the recognition sites for several other FtsZ-interacting proteins, including MinC, ZipA and FtsA. One region is located 30 residues away from the C-terminus in the unstructured linker region that connects the polymerization domain to the C-terminal region. We identified two discrete regions of FtsZ important for degradation of both FtsZ monomers and polymers by ClpXP in vitro. To better understand substrate selection by ClpXP, we engineered FtsZ mutant proteins containing amino acid substitutions or deletions near the FtsZ C-terminus. The FtsZ monomer is composed of an N-terminal polymerization domain, an unstructured linker region and a C-terminal conserved region. Install ADB & FastBoot Tools in Termux For devices with ARM or ARM64 processors only How to install. FtsZ forms polymers that assemble into a large ring-like structure, termed the Z-ring, during cell division at the site of constriction. One substrate degraded by Escherichia coli ClpXP is FtsZ, an essential cell division protein. ClpXP is a two-component ATP-dependent protease that unfolds and degrades proteins bearing specific recognition signals.
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