Background:We previously identified GAREM1 as a downstream adaptor of the EGF receptor. Results: GAREM2 is a brain-specific GAREM subtype that is also tyrosine-phosphorylated and binds Grb2. Conclusion: GAREM2 is a regulator of neurite outgrowth of neuroblastoma cells in the presence of IGF-1. Significance: This study demonstrates the biological function of the GAREM family proteins, including their expression and subcellular localization.
The Mn4CaO5 cluster of photosystem II (PSII) advances sequentially through five oxidation states (S0 to S4). Under the enzyme cycle, two water molecules are oxidized, O2 is generated and four protons are released into the lumen. Umena et al. (2011) have proposed that, with other charged amino acids, the R323 residue of the D1 protein could contribute to regulate a proton egress pathway from the Mn4CaO5 cluster and TyrZ via a proton channel identified from the 3D structure. To test this suggestion, a PsbA3/R323E site‐directed mutant has been constructed and the properties of its PSII have been compared to those of the PsbA3‐PSII by using EPR spectroscopy, polarography, thermoluminescence and time‐resolved UV–visible absorption spectroscopy. Neither the oscillations with a period four nor the kinetics and S‐state‐dependent stoichiometry of the proton release were affected. However, several differences have been found: (1) the P680+ decay in the hundreds of ns time domain was much slower in the mutant, (2) the S2QA−/DCMU and S3QA−/DCMU radiative charge recombination occurred at higher temperatures and (3) the S0TyrZ•, S1TyrZ•, S2TyrZ• split EPR signals induced at 4.2 K by visible light from the S0TyrZ, S1TyrZ, S2TyrZ, respectively, and the (S2TyrZ•)' induced by NIR illumination at 4.2 K of the S3TyrZ state differed. It is proposed that the R323 residue of the D1 protein interacts with TyrZ likely via the H‐bond network previously proposed to be a proton channel. Therefore, rather than participating in the egress of protons to the lumen, this channel could be involved in the relaxations of the H‐bonds around TyrZ by interacting with the bulk, thus tuning the driving force required for TyrZ oxidation.
Escherichia coli failed to survive after transformation with a Streptococcus intermedius histone-like protein gene (Si-hlp) and its promoter-harbored plasmid. The promoter function of Si-hlp in E. coli was determined using enhanced green fluorescence protein (egfp) gene as a reporter. The inhibitory effect of Si-HLP on E. coli viability was verified by a tetracycline-inducible gene expression system. Further study suggested that Si-HLP may alter the bacterial nucleoid structure, leading to the growth inhibition of E. coli.
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