PMID- 33174898
OWN - NLM
STAT- MEDLINE
DCOM- 20211102
LR  - 20211224
IS  - 1756-591X (Electronic)
IS  - 1756-5901 (Print)
IS  - 1756-5901 (Linking)
VI  - 12
IP  - 12
DP  - 2020 Dec 23
TI  - Vibrio cholerae FeoB hydrolyzes ATP and GTP in vitro in the absence of 
      stimulatory factors.
PG  - 2065-2074
LID - 10.1039/d0mt00195c [doi]
AB  - Feo is the most widely conserved system for ferrous iron transport in 
      prokaryotes, and it is important for virulence in some pathogens. However, its 
      mechanism of iron transport is not fully understood. In this study, we used 
      full-length Vibrio cholerae FeoB (VcFeoB) as a model system to study whether its 
      enzymatic activity is affected by regulatory factors commonly associated with 
      FeoB proteins from other species or with G-proteins that have homology to FeoB. 
      VcFeoB showed a higher rate of hydrolysis of both ATP and GTP than its N-terminal 
      domain alone; likewise, ions such as K+ and Fe2+ did not modulate its nucleotide 
      hydrolysis. We also showed that the three V. cholerae Feo proteins (FeoA, FeoB, 
      and FeoC) work in a 1 : 1 : 1 molar ratio in vivo. Although both FeoA and FeoC 
      are required for Feo-mediated iron transport, neither of these proteins affected 
      the VcFeoB NTPase rate. These results are consistent with an active transport 
      mechanism independent of stimulatory factors and highlight the importance of 
      using full-length FeoB proteins as a reliable proxy to study Feo-mediated iron 
      transport in vitro.
FAU - Gomez-Garzon, Camilo
AU  - Gomez-Garzon C
AD  - Department of Molecular Biosciences, University of Texas at Austin, Austin, TX 
      78712, USA. payne@utexas.edu.
FAU - Payne, Shelley M
AU  - Payne SM
LA  - eng
GR  - R01 AI091957/AI/NIAID NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PL  - England
TA  - Metallomics
JT  - Metallomics : integrated biometal science
JID - 101478346
RN  - 0 (Bacterial Proteins)
RN  - 86-01-1 (Guanosine Triphosphate)
RN  - 8L70Q75FXE (Adenosine Triphosphate)
RN  - E1UOL152H7 (Iron)
RN  - RWP5GA015D (Potassium)
SB  - IM
MH  - Adenosine Triphosphate/*metabolism
MH  - Bacterial Proteins/*metabolism
MH  - Cholera/microbiology
MH  - Guanosine Triphosphate/*metabolism
MH  - Humans
MH  - Hydrolysis
MH  - Iron/metabolism
MH  - Potassium/metabolism
MH  - Vibrio cholerae/*metabolism
PMC - PMC7769900
MID - NIHMS1646566
COIS- Conflicts of interest There are no conflicts to declare.
EDAT- 2020/11/12 06:00
MHDA- 2021/11/03 06:00
PMCR- 2021/12/23
CRDT- 2020/11/11 12:12
PHST- 2020/11/12 06:00 [pubmed]
PHST- 2021/11/03 06:00 [medline]
PHST- 2020/11/11 12:12 [entrez]
PHST- 2021/12/23 00:00 [pmc-release]
AID - 10.1039/d0mt00195c [doi]
PST - ppublish
SO  - Metallomics. 2020 Dec 23;12(12):2065-2074. doi: 10.1039/d0mt00195c.