Longitudinal axis thickenings in whole-mount spreads of synaptonemal complexes from Tradescantia

The whole-mount spreading technique was used to examine the chromosome complement in ten zygotene nuclei of Tradescantia ohiensis var. paludosa. Spread preparations have normal synaptonemal complex (SC) morphology. Neither kinetochores nor recombination nodules were regularly visible. Cloudlike structures (LFSs) 2–6 m in diameter were sometimes associated with SC and with unsynapsed lateral components (LCs). They differed in number and location in different nuclei. Thickenings of the lateral elements and LCs were observed in mid through late zygotene nuclei. These longitudinal axis thickenings (LATS) were distributed fairly uniformly amongst the chromosomes and occurred in both synapsed and unsynapsed regions. There was a stage-dependent increase in the number and size of LATS. They were nonrandomly distributed along the length of a chromosome, being more frequent in synapsed areas, especially near junctions with unsynapsed regions.     

Cytochalasin B inhibition of endothelial proliferation at wound edges in vitro

Cytochalasin B prevents both migration and wound-associated replication when applied to wounded monolayers of bovine endothelium in tissue culture. The normal low background rate of replication in undisturbed areas of the cultures is not inhibited by cytochalasin B. These results suggest that some form of movement may be required for initiation of wound-associated replication by endothelial cells.     

Nosocomial transmission of group B streptococci.

The acquisition of group B streptococci by babies in a special-care baby unit and two postnatal wards was investigated over a six-month period using serology and phage typing. Sixty-three culture-positive babies were identified in the postnatal wards, one-third of whom had been born to mothers who were not carrying the organism in the genital tract or anorectal area during labour. A non-maternal source was identified for 14 of these 21 infants: either colonised mothers and babies in the same ward or, on one occasion, a member of the hospital staff. In the special-care baby unit, however, only one instance of nosocomial acquisition of group B streptococci was recorded despite a high prevalence of colonisation in the staff on the unit and the presence of heavily colonised babies. The results of this survey suggest that although sepsis caused by group B streptococci may be the result of nosocomial transmission, this may be prevented by careful attention to hygiene.     

High affinity divalent cation exchange on actin. Association rate measurements support the simple competitive model

Each actin molecule has one high affinity site which binds a divalent cation. It has been proposed that an isomerization of the actin molecule is involved in divalent cation exchange at this site ("isomerization model," Frieden, C. (1982) J. Biol. Chem. 257, 2882-2886); we have maintained that exchange is by a simple competitive mechanism (Estes, J. E., Selden, L. A., and Gershman, L. C. (1987) J. Biol. Chem. 262, 4952-4957). Here, using fluorescent-labeled actin, we measure the apparent rate constant for exchange (kapp) as a function of the ratio of free Ca2+ and Mg2+ concentrations, ([Ca]/[Mg]), and show that both models are consistent with the data. The major parameter controlling this relationship in the simple competitive exchange model, the ratio of the association rate constants for Ca2+ and Mg2+ to actin (kCa/kMg), is found to have a value of about 90. We have verified this parameter by direct measurements of kCa and kMg, finding that kCa = 1.9 x 10(7) M-1 s-1 and kMg = 2.3 x 10(5) M-1 s-1, consistent with the characteristics of the Ca2+ and Mg2+ aquo ions. The corresponding parameter derived from the isomerization model is not verifiable. We conclude that high affinity divalent cation exchange on actin proceeds by a simple competitive mechanism.     

Antibodies directed against a meiosis-specific,chromatin-associated protein identify conserved meiotic epitopes

The molecular mechanisms by which meiotic events are regulated are at present unknown. To approach this problem, we have exploited the natural synchrony of Lilium meiocytes to compare the nuclear protein profiles of a variety of stages of meiosis. This approach has facilitated the identification of a number of nuclear proteins that appear and disappear in a stagespecific fashion. Here we report the presence of an abundant nuclear protein that first appears during premeiotic interphase, a period during which the irreversible commitment to meiosis occurs. Antibodies directed against this protein demonstrate its meiosis specificity as well as conservation of the epitope(s) in both mono-and dicotyledonous plant species. Chromatin fractionation studies indicate that this protein, which we have termed meiotin-1, is associated with strings of nucleosomes. Implications for meiotic chromatin packaging and chromosome structure are discussed.by J.H. Taylor