Leu65 in the heme distal side is critical for the stability of the Fe(II)–O2 complex of YddV, a globin-coupled oxygen sensor diguanylate cyclase

Nakajima, Kyosuke; Kitanishi, Kenichi; Kobayashi, Kazuo; Kobayashi, Nagao; Igarashi, Jun–ichi; Shimizu, Tôru

doi:10.1016/j.jinorgbio.2011.09.019

Cited by 23 publications

(32 citation statements)

References 37 publications

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“…coli [10, 44], and the results were, for the most part, in agreement with what we observed for similar mutant proteins expressed in S . typhimurium .…”

Section: Resultssupporting

confidence: 91%

The importance of conserved amino acids in heme-based globin-coupled diguanylate cyclases

et al. 2017

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Globin-coupled diguanylate cyclases contain globin, middle, and diguanylate cyclase domains that sense O2 to synthesize c-di-GMP and regulate bacterial motility, biofilm formation, and virulence. However, relatively few studies have extensively examined the roles of individual residues and domains of globin-coupled diguanylate cyclases, which can shed light on their signaling mechanisms and provide drug targets. Here, we report the critical residues of two globin-coupled diguanylate cyclases, EcGReg from Escherichia coli and BpeGReg from Bordetella pertussis, and show that their diguanylate cyclase activity requires an intact globin domain. In the distal heme pocket of the globin domain, residues Phe42, Tyr43, Ala68 (EcGReg)/Ser68 (BpeGReg), and Met69 are required to maintain full diguanylate cyclase activity. The highly conserved amino acids His223/His225 and Lys224/Lys226 in the middle domain of EcGReg/BpeGReg are essential to diguanylate cyclase activity. We also identified sixteen important residues (Leu300, Arg306, Asp333, Phe337, Lys338, Asn341, Asp342, Asp350, Leu353, Asp368, Arg372, Gly374, Gly375, Asp376, Glu377, and Phe378) in the active site and inhibitory site of the diguanylate cyclase domain of EcGReg. Moreover, BpeGReg266 (residues 1–266) and BpeGReg296 (residues 1–296), which only contain the globin and middle domains, can inhibit bacterial motility. Our findings suggest that the distal residues of the globin domain affect diguanylate cyclase activity and that BpeGReg may interact with other c-di-GMP-metabolizing proteins to form mixed signaling teams.

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“…coli [10, 44], and the results were, for the most part, in agreement with what we observed for similar mutant proteins expressed in S . typhimurium .…”

Section: Resultssupporting

confidence: 91%

The importance of conserved amino acids in heme-based globin-coupled diguanylate cyclases

et al. 2017

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“…To date, GCS proteins with diguanylate cyclase (DGC) output domains have been characterized from E. coli ( Ec DosC), Shewanella putrefaciens (DosD), Bordetella pertussis ( Bpe GReg), Pectobacterium carotovorum ( Pcc GCS), Desulfotalia psychrophila (HemDGC), and Azotobacter vinelandii ( Av GReg) (Burns et al, 2014; Burns et al, 2016; Donné et al, 2016; Kitanishi et al, 2010; Lambry et al, 2016; Nakajima et al, 2012; Sawai et al, 2010; Tagliabue et al, 2010; Tarnawski et al, 2015; Tuckerman et al, 2009; Wan et al, 2009; Wu et al, 2013). All of these DGC-containing GCS proteins have a linking middle domain between the N-terminal sensor globin and C-terminal DGC domain.…”

Section: Diguanylate Cyclase-containing Gcs Proteinsmentioning

confidence: 99%

“…L65 also serves to limit access to the distal pocket and ligand rebinding within the pocket, with mutations resulting in increased ligand association rates. In addition, blocking water access to the distal pocket decreases auto-oxidation of the heme, stabilizing the Fe II -O 2 state of Ec DosC (Nakajima et al, 2012). …”

Section: Diguanylate Cyclase-containing Gcs Proteinsmentioning

confidence: 99%

Mechanism and Role of Globin-Coupled Sensor Signalling

Walker

Rivera

Weinert

2017

Advances in Microbial Physiology

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The discovery of the globin-coupled sensor (GCS) family of haem proteins has provided new insights into signalling proteins and pathways by which organisms sense and respond to changing oxygen levels. GCS proteins consist of a sensor globin domain linked to a variety of output domains, suggesting roles in controlling numerous cellular pathways, and behaviours in response to changing oxygen concentration. Members of this family of proteins have been identified in the genomes of numerous organisms and characterization of GCS with output domains, including methyl accepting chemotaxis proteins, kinases, and diguanylate cyclases, have yielded an understanding of the mechanism by which oxygen controls activity of GCS protein output domains, as well as downstream proteins and pathways regulated by GCS signalling. Future studies will expand our understanding of these proteins both in vitro and in vivo, likely demonstrating broad roles for GCS in controlling oxygen-dependent microbial physiology and phenotypes.

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“…Full-length Enzymes Are Dimers or Tetramers-The DGCGCSs identified and characterized to date, such as HemAT-Bs (22), AvGReg (35), BpeGReg (36), HemDGC (37), and YddV (32,38,39), are dimers or tetramers. Such an arrangement suggests that each subunit catalyzes the cyclization reaction possibly in synergy with other subunits in the dimer/tetramer.…”

Section: The Heme Fe(ii)-o 2 Complex Is Stable With a Low Autoxidatiomentioning

confidence: 99%

Heme-based Globin-coupled Oxygen Sensors: Linking Oxygen Binding to Functional Regulation of Diguanylate Cyclase, Histidine Kinase, and Methyl-accepting Chemotaxis

Martínková

Kitanishi

Shimizu

2013

Journal of Biological Chemistry

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107

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An emerging class of novel heme-based oxygen sensors containing a globin fold binds and senses environmental O 2 via a heme iron complex. Structure-function relationships of oxygen sensors containing a heme-bound globin fold are different from those containing heme-bound PAS and GAF folds. It is thus worth reconsidering from an evolutionary perspective how heme-bound proteins with a globin fold similar to that of hemoglobin and myoglobin could act as O 2 sensors. Here, we summarize the molecular mechanisms of heme-based oxygen sensors containing a globin fold in an effort to shed light on the O 2 -sensing properties and O 2 -stimulated catalytic enhancement observed for these proteins.

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Leu65 in the heme distal side is critical for the stability of the Fe(II)–O2 complex of YddV, a globin-coupled oxygen sensor diguanylate cyclase

Cited by 23 publications

References 37 publications

The importance of conserved amino acids in heme-based globin-coupled diguanylate cyclases

The importance of conserved amino acids in heme-based globin-coupled diguanylate cyclases

Mechanism and Role of Globin-Coupled Sensor Signalling

Heme-based Globin-coupled Oxygen Sensors: Linking Oxygen Binding to Functional Regulation of Diguanylate Cyclase, Histidine Kinase, and Methyl-accepting Chemotaxis

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