TY  - JOUR
A1  - Salzer, Ralf
A1  - Herzberg, Martin
A1  - Nies, Dietrich H.
A1  - Joos, Friederike
A1  - Rathmann, Barbara
A1  - Thielmann, Yvonne
A1  - Averhoff, Beate
T1  - Zinc and ATP Binding of the Hexameric AAA-ATPase PilF from Thermus thermophilus
T2  - Journal of biological chemistry
N2  - The traffic AAA-ATPase PilF is essential for pilus biogenesis and natural transformation of Thermus thermophilus HB27. Recently, we showed that PilF forms hexameric complexes containing six zinc atoms coordinated by conserved tetracysteine motifs. Here we report that zinc binding is essential for complex stability. However, zinc binding is neither required for pilus biogenesis nor natural transformation. A number of the mutants did not exhibit any pili during growth at 64 °C but still were transformable. This leads to the conclusion that type 4 pili and the DNA translocator are distinct systems. At lower growth temperatures (55 °C) the zinc-depleted multiple cysteine mutants were hyperpiliated but defective in pilus-mediated twitching motility. This provides evidence that zinc binding is essential for the role of PilF in pilus dynamics. Moreover, we found that zinc binding is essential for complex stability but dispensable for ATPase activity. In contrast to many polymerization ATPases from mesophilic bacteria, ATP binding is not required for PilF complex formation; however, it significantly increases complex stability. These data suggest that zinc and ATP binding increase complex stability that is important for functionality of PilF under extreme environmental conditions.
Y1  - 2021
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/76987
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-769877
SN  - 0021-9258
VL  - 289.2014
IS  - 44
SP  - 30343
EP  - 30354
PB  - American Society for Biochemistry and Molecular Biology Publications
CY  - Bethesda, Md
ER  -