PMID- 38264987
OWN - NLM
STAT- MEDLINE
DCOM- 20240318
LR  - 20240318
IS  - 1520-4995 (Electronic)
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 63
IP  - 4
DP  - 2024 Feb 20
TI  - Gas-Selective Catalytic Regulation by a Newly Identified Globin-Coupled Sensor 
      Phosphodiesterase Containing an HD-GYP Domain from the Human Pathogen Vibrio 
      fluvialis.
PG  - 523-532
LID - 10.1021/acs.biochem.3c00484 [doi]
AB  - Globin-coupled sensors constitute an important family of heme-based gas sensors, 
      an emerging class of heme proteins. In this study, we have identified and 
      characterized a globin-coupled sensor phosphodiesterase containing an HD-GYP 
      domain (GCS-HD-GYP) from the human pathogen Vibrio fluvialis, which is an 
      emerging foodborne pathogen of increasing public health concern. The amino acid 
      sequence encoded by the AL536_01530 gene from V. fluvialis indicated the presence 
      of an N-terminal globin domain and a C-terminal HD-GYP domain, with HD-GYP 
      domains shown previously to display phosphodiesterase activity toward 
      bis(3',5')-cyclic dimeric guanosine monophosphate (c-di-GMP), a bacterial second 
      messenger that regulates numerous important physiological functions in bacteria, 
      including in bacterial pathogens. Optical absorption spectral properties of 
      GCS-HD-GYP were found to be similar to those of myoglobin and hemoglobin and of 
      other bacterial globin-coupled sensors. The binding of O(2) to the Fe(II) heme 
      iron complex of GCS-HD-GYP promoted the catalysis of the hydrolysis of c-di-GMP 
      to its linearized product, 5'-phosphoguanylyl-(3',5')-guanosine (pGpG), whereas 
      CO and NO binding did not enhance the catalysis, indicating a strict 
      discrimination of these gaseous ligands. These results shed new light on the 
      molecular mechanism of gas-selective catalytic regulation by globin-coupled 
      sensors, with these advances apt to lead to a better understanding of the family 
      of globin-coupled sensors, a still growing family of heme-based gas sensors. In 
      addition, given the importance of c-di-GMP in infection and virulence, our 
      results suggested that GCS-HD-GYP could play an important role in the ability of 
      V. fluvialis to sense O(2) and NO in the context of host-pathogen interactions.
FAU - Kitanishi, Kenichi
AU  - Kitanishi K
AUID- ORCID: 0000-0002-2110-8104
AD  - Department of Chemistry, Faculty of Science, Tokyo University of Science, 1-3 
      Kagurazaka, Shinjuku-ku, Tokyo 162-8601, Japan.
FAU - Aoyama, Nao
AU  - Aoyama N
AD  - Department of Chemistry, Graduate School of Science, Tokyo University of Science, 
      1-3 Kagurazaka, Shinjuku-ku, Tokyo 162-8601, Japan.
FAU - Shimonaka, Motoyuki
AU  - Shimonaka M
AD  - Department of Chemistry, Faculty of Science, Tokyo University of Science, 1-3 
      Kagurazaka, Shinjuku-ku, Tokyo 162-8601, Japan.
LA  - eng
PT  - Journal Article
DEP - 20240124
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - EC 3.1.4.- (Phosphoric Diester Hydrolases)
RN  - 9004-22-2 (Globins)
RN  - 0 (Bacterial Proteins)
RN  - H2D2X058MU (Cyclic GMP)
RN  - 42VZT0U6YR (Heme)
RN  - Vibrio fluvialis
SB  - IM
MH  - Humans
MH  - *Phosphoric Diester Hydrolases/genetics
MH  - *Globins/genetics
MH  - Bacterial Proteins/chemistry
MH  - Catalysis
MH  - Cyclic GMP/metabolism
MH  - Heme/chemistry
MH  - *Vibrio
PMC - PMC10882959
COIS- The authors declare no competing financial interest.
EDAT- 2024/01/24 12:43
MHDA- 2024/03/18 06:43
PMCR- 2024/02/22
CRDT- 2024/01/24 08:55
PHST- 2024/03/18 06:43 [medline]
PHST- 2024/01/24 12:43 [pubmed]
PHST- 2024/01/24 08:55 [entrez]
PHST- 2024/02/22 00:00 [pmc-release]
AID - 10.1021/acs.biochem.3c00484 [doi]
PST - ppublish
SO  - Biochemistry. 2024 Feb 20;63(4):523-532. doi: 10.1021/acs.biochem.3c00484. Epub 
      2024 Jan 24.