Signals from micromere descendants play a crucial role in sea urchin development. In this study, we demonstrate that these micromere descendants express HpTb, a T-brain homolog of Hemicentrotus pulcherrimus. HpTb is expressed transiently from the hatched blastula stage through the mesenchyme blastula stage to the gastrula stage. By a combination of embryo microsurgery and antisense morpholino experiments, we show that HpTb is involved in the production of archenteron induction signals. However, HpTb is not involved in the production of signals responsible for the specification of secondary mesenchyme cells, the initial specification of primary mesenchyme cells, or the specification of endoderm. HpTb expression is controlled by nuclear localization of beta-catenin, suggesting that HpTb is in a downstream component of the Wnt signaling cascade. We also propose the possibility that HpTb is involved in the cascade responsible for the production of signals required for the spicule formation as well as signals from the vegetal hemisphere required for the differentiation of aboral ectoderm.
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http://dx.doi.org/10.1242/dev.129.22.5205 | DOI Listing |
Spectrochim Acta A Mol Biomol Spectrosc
October 2022
Department of Chemistry, Central University of Haryana, Mahendergarh 123031, India. Electronic address:
Bridged dinuclear metal complexes have fascinated scientists worldwide, and remarkable success has been achieved to unravel the electronic structures, structure-function relationship, coordination environments, and fine mechanistic details of the enzymes owing to the repercussion of biomimetic studies carried out on dinuclear model systems. Molecular level study of these systems integrated with spectroscopic study helps in gaining deep insights about structural and electronic aspects of natural enzymatic systems. Considering the same, here first time we report DFT study on bridged non-heme metal complexes based on N-Et-HPTB ligand system containing homovalent (MM); {[(Mn)(OCCH)(N-Et-HPTB)]; Species I), [(Fe)(OCCH)(N-Et-HPTB)]; Species II), [(Co)(OCCH)(N-Et-HPTB)]; Species III)} and heterovalent (MM): {[(Mn)(Mn)(O)(N-Et-HPTB)]; Species Ia) [(Fe)(Fe)(O)(N-Et-HPTB)]; Species IIa) and [(Co)(Co)(O)(N-Et-HPTB)]; Species IIIa)} dinuclear metal centres.
View Article and Find Full Text PDFBiofilm
December 2021
Department of Biological Sciences, Binghamton University, Binghamton, NY, USA.
The orphan sensor SagS (PA2824) was initially reported as one of three orphan sensor kinases capable of activating HptB, a component of the HptB signaling pathway that intersects with the Gac/Rsm signaling pathway and fine-tunes motility and pathogenesis. Since then, this orphan sensor has been reported to be involved in other, unorthodox signaling pathways serving additional functions. The present review is aimed at summarizing the various functions of SagS, with an emphasis on its toggle or dual switch functions, and highlighting the role of SagS as a hub at which the various signaling pathways intersect, to regulate the transition from the planktonic to the sessile mode of growth, as well as the transition of surface-associated cells to a drug tolerant state.
View Article and Find Full Text PDFIUCrJ
September 2020
Department of Biotechnology and Bioindustry Sciences, National Cheng Kung University, Tainan City 701, Taiwan.
J Am Chem Soc
April 2020
School of Chemical Sciences, Indian Association for the Cultivation of Science, 2A & 2B Raja S. C. Mullick Road, Jadavpur, Kolkata 700032, West Bengal, India.
The reduction of NO to NO by flavodiiron nitric oxide reductases (FNORs) is related to the disruption of the defense mechanism in mammals against invading pathogens. The proposed mechanism for this catalytic reaction involves both nonheme mono- and dinitrosyl diiron(II) species as the key intermediates. Recently, we reported an initial account for NO reduction activity of an unprecedented mononitrosyl diiron(II) complex, [Fe(-Et-HPTB)(NO)(DMF)](BF) () (-Et-HPTB is the anion of N,N,N',N'-tetrakis(2-(l-ethylbenzimidazolyl))-2-hydroxy-1,3-diaminopropane; DMF = dimethylformamide) with [Fe{FeNO}] formulation [Jana et al.
View Article and Find Full Text PDFPLoS Genet
October 2016
MRC Centre for Molecular Microbiology and Infection, Department of Life Sciences, Imperial College London, London, United Kingdom.
The molecular basis of second messenger signaling relies on an array of proteins that synthesize, degrade or bind the molecule to produce coherent functional outputs. Cyclic di-GMP (c-di-GMP) has emerged as a eubacterial nucleotide second messenger regulating a plethora of key behaviors, like the transition from planktonic cells to biofilm communities. The striking multiplicity of c-di-GMP control modules and regulated cellular functions raised the question of signaling specificity.
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