Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDP.

Ffh is a component of a bacterial ribonucleoprotein complex homologous to the signal recognition particle (SRP) of eukaryotes. It comprises three domains that mediate both binding to the hydrophobic signal sequence of the nascent polypeptide and the GTP-dependent interaction of Ffh with a structurally homologous GTPase of the SRP receptor. The X-ray structures of the two-domain 'NG' GTPase of Ffh in complex with Mg2+GDP and GDP have been determined at 2.0 A resolution. The structures explain the low nucleotide affinity of Ffh and locate two regions of structural mobility at opposite sides of the nucleotide-binding site. One of these regions includes highly conserved sequence motifs that presumably contribute to the structural trigger signaling the GTP-bound state. The other includes the highly conserved interface between the N and G domains, and supports the hypothesis that the N domain regulates or signals the nucleotide occupancy of the G domain.     

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Occurrence of multiple-antibiotic-resistant enteric bacteria in domestic sewage and oxidation lagoons

The coliform bacterial population in the Grand Forks, N.Dak. sewage system was examined for multiple-antibiotic-resistant organisms over a 1-year period. Multiple-antibiotic-resistant coliforms were found to be common in the sewage, and their numbers remained fairly constant relative to the total coliform population throughout the year. Resistance to kanamycin, tetracycline, and ampicillin was found to be transferable at variable rates. Transfer rates were found to be temperature sensitive and were optimal at 35 degrees C. Although 75% of the multiple-antibiotic-resistant coliforms were capable of transferring resistance at some level, only 25% were capable of transferring resistance at rates greater than 10(-3) transconjugants per initial donor.     

Release of pituitary melanocyte-stimulating hormone by the oxytocin fragment, H-Cys-Tyr-Ile-Gln-Asn-Oh

The effect of the pentapeptide H-Cys-Tyr-Ile-Gln-Asn-OH to act like melanocyte-stimulating hormone-releasing factor (MSH-RF) was studied. This peptide decreases at ng amounts the MSH content of the rat pituitary and increases plasma MSH concentration. This agent also stimulates the release of MSH in animals with eminence lesion, indicating a direct action of the pentapeptide on the gland.     

K+(Rb+) and Ca2+ fluxes in young winter wheat plants exposed to sub-zero temperatures

Ice crystal formation temperature was determined in the region of the crown in one group of 7-day-old intact unhardened high-salt plants of winter wheat (Triticum aestivum L. cv. Weibulls Starke II) with TA (Thermal Analysis) and DTA (Differential Thermal Analysis) methods. After exposure of another group of plants, grown for the first 7 days in the same way as the first group, to various sub-zero temperatures (-1 to 5°C), influx in roots of Rb⁺(⁸⁶Rb⁺) and Ca²⁺(⁴⁵Ca²⁺) and contents of K⁺ and Ca²⁺ were determined at intervals during 7 days of recovery. Ice crystal formation in the crown tissue was probably extracellular and took place at about -4°C. There was a large loss of K⁺ from the roots after treatment at sub-zero temperatures. This loss increased as the temperature of the sub-zero treatment decreased. During recovery, roots of plants exposed to -1, -2 and -3°C gradually reabsorbed K⁺. Reabsorption of K⁺ in roots of plants exposed to -4°C was greatly impaired. Rb⁺ influx decreased and Ca²⁺ influx increased after sub-zero temperature treatments of the plants. Active Rb⁺ influx mechanisms and active extrusion of Ca²⁺ were impaired or irreversibly damaged by the exposure. While Rb⁺ influx mechanisms were apparently repaired during recovery in plants exposed to temperatures down to -3°C, Ca²⁺ extrusion mechanisms were not. The temperature for ice crystal formation in the region of the crown tissue coincides with the temperature at which the plants lost the ability to reabsorb K⁺ and to repair Rb⁺ influx mechanisms during the recovery period. Plants were lethally damaged at temperatures below ?4°C.     

Modulation of murine hemopoiesis in vivo by a synthetic hemoregulatory pentapeptide (HP 5b)

Abstract. Degeneration of the archenteron in middle gastrulae occurred in the presence of α,α'-dipyridyl or Zn²⁺, inhibitors of prolyl hydroxylase. In the presence of these substances the archenteron degenerated and was eventually destroyed. Adding Fe²⁺ to the embryo culture containing α,α'-dipyridyl protected the archenteron from further degeneration, but the collapsed archenteron was not restored to the upright position. At the late gastrula stage, α,α'-dipyridyl did not cause the degeneration of the archenteron. Treatment of the embryos by α,α'-dipyridyl, starting at the swimming blastula stage, resulted in the production of many mesenchyme-like cells but archenteron was not produced in the embryos. Addition of Fe²⁺ to α,α'-dipyridyl culture, just before the beginning of gastrulation of normal embryos, resulted in the formation of normal archenteron. α,α'-Dipyridyl inhibited hydroxylation of proline residues of collagen in sea urchin embryos and Fe²⁺ prevented the inhibition by α,α'-dipyridyl. Respiration was not inhibited by α,α'-dipyridyl.     

EXO5-DNA structure and BLM interactions direct DNA resection critical for ATR-dependent replication restart

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