Expanding the Kinome World: A New Protein Kinase Family Widely Conserved in Bacteria

Nguyen, Hai Duc; Khoury, Takla El; Guiral, Sébastien; Laaberki, Maria-Halima; Candusso, Marie-Pierre; Galisson, Frédéric; Foucher, Anne-Emmanuelle; Kesraoui, Salsabil; Ballut, Lionel; Vallet, Sylvain D.; Orelle, Cédric; Zucchini, Laure; Martin, Juliette; Page, Adeline; Attieh, Jihad; Aghajari, Nushin; Grangeasse, Christophe; Jault, Jean‐Michel

doi:10.1016/j.jmb.2017.08.016

Cited by 25 publications

(52 citation statements)

References 75 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The overall structures of Tm TsaB, Tm TsaD and Tm TsaE in the complex are the same as those of the individual proteins ( Tm TsaB) or orthologues ( H. influenza (Hi) - and B. subtilis(Bs) TsaE and St(S. typhimurium), Ec(E. coli) TsaD and Kae1) ( Supplementary Table S1 ) ( 28 , 29 ) ( 49 ). Sequence alignments with superposed secondary structure assignments of a few TsaB, TsaD and TsaE orthologues are represented in Supplementary Figure S1 .…”

Section: Resultsmentioning

confidence: 91%

“…The need of ATP-hydrolysis for t 6 A biosynthesis in bacteria is presently unclear. The structure of TsaE in complex with ADP revealed the presence of a Walker A motif and two switch regions that are characteristic of P-loop GTP hydrolases ( 28 , 29 ) In presence of non-hydrolysable ATP analogues, Ec TsaB, Ec TsaD and Ec TsaE form a Ec TsaBDE complex with 1:1:1 stoichiometry ( 22 ). From small angle X-ray scattering (SAXS) measurements and biochemical data, it was proposed that Ec TsaE binds at the Ec TsaBD interface ( 22 ).…”

Section: Introductionmentioning

confidence: 99%

“…The essential character of TsaE for bacterial survival, the presence of its encoding gene in all pathogenic bacterial genomes and the absence of human orthologues, makes TsaE an attractive antibacterial drug target ( 29 , 32 ). However, its role in the t 6 A process remains poorly understood, mainly because there is no high resolution structural information on its interactions with TsaBD.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

The structure of the TsaB/TsaD/TsaE complex reveals an unexpected mechanism for the bacterial t6A tRNA-modification

Missoury

Plancqueel

Sierra-Gallay

et al. 2018

Nucleic Acids Research

View full text Add to dashboard Cite

The universal N6-threonylcarbamoyladenosine (t6A) modification at position A37 of ANN-decoding tRNAs is essential for translational fidelity. In bacteria the TsaC enzyme first synthesizes an l-threonylcarbamoyladenylate (TC-AMP) intermediate. In cooperation with TsaB and TsaE, TsaD then transfers the l-threonylcarbamoyl-moiety from TC-AMP onto tRNA. We determined the crystal structure of the TsaB–TsaE–TsaD (TsaBDE) complex of Thermotoga maritima in presence of a non-hydrolysable AMPCPP. TsaE is positioned at the entrance of the active site pocket of TsaD, contacting both the TsaB and TsaD subunits and prohibiting simultaneous tRNA binding. AMPCPP occupies the ATP binding site of TsaE and is sandwiched between TsaE and TsaD. Unexpectedly, the binding of TsaE partially denatures the active site of TsaD causing loss of its essential metal binding sites. TsaE interferes in a pre- or post-catalytic step and its binding to TsaBD is regulated by ATP hydrolysis. This novel binding mode and activation mechanism of TsaE offers good opportunities for antimicrobial drug development.

show abstract

Section: Resultsmentioning

confidence: 91%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

The structure of the TsaB/TsaD/TsaE complex reveals an unexpected mechanism for the bacterial t6A tRNA-modification

Missoury

Plancqueel

Sierra-Gallay

et al. 2018

Nucleic Acids Research

View full text Add to dashboard Cite

show abstract

“…85,86 Immunoglobulins on the other hand are prone to aggregation. 87,88 Since the nature of organism or antigen is varied, various types of excipients are used to stabilize them and their ability to provide safety, stability and storage are controlled through the guidelines set by US Food and Drug administration. 89 One such potential excipient that may help to overcome the above mentioned issues is the use of osmolytes in formulations.…”

Section: Osmolytes In Vaccine Flocculationmentioning

confidence: 99%

Osmolytes in vaccine production, flocculation and storage: a critical review

Hasan

Kumari

Devi

et al. 2018

Human Vaccines & Immunotherapeutics

View full text Add to dashboard Cite

Small molecule osmolytes, responsible for protecting stresses have long been known to rescue proteins and enzymes from loss of function. In addition to protecting macromolecules integrity, many osmolytes also act as potential antioxidant and also help to prevent protein aggregation, amyloid formation or misfolding, and therefore are considered promising molecules for neurodegenerative and many other genetic diseases. Osmolytes are also known to be involved in the regulation of several key immunological processes. In the present review we discuss in detail the effect of these compounds on important aspects of vaccines i.e., increasing the efficiency, production and purification steps. The present review therefore will help researchers to make a better strategy in vaccine production to formulation by incorporating specific and appropriate osmolytes in the processes.

show abstract

“…These include: His kinases, Tyr kinases, Arg kinases, Hanks-type Ser/Thr kinases (STKs) (also commonly named eukaryotic-like STKs), and atypical Ser kinases [ 3 ]. Recently, Nguyen and others [ 10 ] have proposed a new family of protein kinases with a Ser/Thr/Tyr kinase activity, that was previously identified as a family of ATPases. A prototypic member of this family, YdiB from Bacillus subtilis , has a unique ATP-binding fold, not found in the known protein kinases.…”

Section: Introductionmentioning

confidence: 99%

Hanks-Type Serine/Threonine Protein Kinases and Phosphatases in Bacteria: Roles in Signaling and Adaptation to Various Environments

Janczarek

Vinardell

Lipa

et al. 2018

IJMS

View full text Add to dashboard Cite

Reversible phosphorylation is a key mechanism that regulates many cellular processes in prokaryotes and eukaryotes. In prokaryotes, signal transduction includes two-component signaling systems, which involve a membrane sensor histidine kinase and a cognate DNA-binding response regulator. Several recent studies indicate that alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) also play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. Since these enzymes are not DNA-binding proteins, they exert the regulatory role via post-translational modifications of their protein targets. In this review, we summarize the current knowledge of STKs and STPs, and discuss how these enzymes mediate gene expression in prokaryotes. Many studies indicate that regulatory systems based on Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. These data show high complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of TCSs, and the translational machinery occurs. In this regulation, the STK/STP systems have been proved to play important roles.

show abstract

Expanding the Kinome World: A New Protein Kinase Family Widely Conserved in Bacteria

Cited by 25 publications

References 75 publications

The structure of the TsaB/TsaD/TsaE complex reveals an unexpected mechanism for the bacterial t6A tRNA-modification

The structure of the TsaB/TsaD/TsaE complex reveals an unexpected mechanism for the bacterial t6A tRNA-modification

Osmolytes in vaccine production, flocculation and storage: a critical review

Hanks-Type Serine/Threonine Protein Kinases and Phosphatases in Bacteria: Roles in Signaling and Adaptation to Various Environments

Contact Info

Product

Resources

About