3-A resolution structure of a protein with histone-like properties in prokaryotes

The 3-A structure of DNA-binding protein II, which exhibits histone-like properties in bacteria, has been determined. The molecule is dimeric and appears to bind to the phosphate backbone of DNA through two symmetry-related arms. A mechanism by which the protein induces DNA supercoiling is proposed.     

Inhibition of aldose reductase by dihydroflavonols inEngelhardtia chrysolepis and effects on other enzymes

Astilbin and neoastilbin, dihydroflavonol rhamnosides fromEngelhardtia chrysolepis, showed potent inhibition of lens aldose reductase. Kinetic analysis showed astilbin exhibited uncompetitive inhibition against bothdl-glyceraldehyde and NADPH. These taxifolin glycosides were selective inhibitors of aldose reductase with no inhibition of NADH oxidase.     

K_Na_Ca_2_PA和BA对黄化黄瓜子叶中Pchlide生物合成的影响

K~+、Na~+、Ca~(2+)、PA和BA对Pchlide的生物合成均有促进作用,其中以K~+和BA的效果最为显著,能使子叶的Pchlide分别比对照增加了25%和28%.混合使用时效果更佳,交叉试验结果表明,以BA+K~++Na~+的组合最好,Pchlide含量增加了84%,Ca~(2+)在4×10~(-4)mol/L浓度时略呈促进作用,当Ca~(2+)和BA混合使用时,可使Pchlide含量增加31%,较高浓度的PA对Pchlide的积累有促进作用.     

The increase of thiobarbituric acid reacting substances in rats with experimental chronic hypoxia

Summary Feeding under conditions of reduced oxygen supply prompted an increase in serum, arterial and brain tissue levels of thiobarbituric acid (TBA)-reacting substances. These observations indicated the possibility that hypoxia might be one of the factors predisposing to the accumulation of lipid peroxide.     

Renal pressor activity and kidney weight responding to angiotensin in hypertensive rats

Zusammenfassung Angiotensin erniedrigte nur bei ischaemischen Nieren die Reninproduktion und erhöhte parallel dazu das Nierengewicht. Die Angiotensinwirkung ist somit abhängig von der Stoffwechsellage der Niere.

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We are indebted to CIBA, Basel (Switzerland) for their generous supply of synthetic angiotensin II.

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Supported in part by research grant from Japanese Ministry of Education.     

Crystal structure of the MgtE Mg2+ transporter

The magnesium ion Mg2+ is a vital element involved in numerous physiological processes. Mg2+ has the largest hydrated radius among all cations, whereas its ionic radius is the smallest. It remains obscure how Mg2+ transporters selectively recognize and dehydrate the large, fully hydrated Mg2+ cation for transport. Recently the crystal structures of the CorA Mg2+ transporter were reported. The MgtE family of Mg2+ transporters is ubiquitously distributed in all phylogenetic domains, and human homologues have been functionally characterized and suggested to be involved in magnesium homeostasis. However, the MgtE transporters have not been thoroughly characterized. Here we determine the crystal structures of the full-length Thermus thermophilus MgtE at 3.5 A resolution, and of the cytosolic domain in the presence and absence of Mg2+ at 2.3 A and 3.9 A resolutions, respectively. The transporter adopts a homodimeric architecture, consisting of the carboxy-terminal five transmembrane domains and the amino-terminal cytosolic domains, which are composed of the superhelical N domain and tandemly repeated cystathionine-beta-synthase domains. A solvent-accessible pore nearly traverses the transmembrane domains, with one potential Mg2+ bound to the conserved Asp 432 within the pore. The transmembrane (TM)5 helices from both subunits close the pore through interactions with the 'connecting helices', which connect the cystathionine-beta-synthase and transmembrane domains. Four putative Mg2+ ions are bound at the interface between the connecting helices and the other domains, and this may lock the closed conformation of the pore. A structural comparison of the two states of the cytosolic domains showed the Mg2+-dependent movement of the connecting helices, which might reorganize the transmembrane helices to open the pore. These findings suggest a homeostasis mechanism, in which Mg2+ bound between cytosolic domains regulates Mg2+ flux by sensing the intracellular Mg2+ concentration. Whether this presumed regulation controls gating of an ion channel or opening of a secondary active transporter remains to be determined.