Temperature sensitivity of complementation at the Maroonlike eye color locus in Drosophila melanogaster

Summary In contrast to the wild-type eye color seen when Drosophila melanogaster heterozygous for mal ¹/mal ^F1 are cultured at 25 C, a mutant eye color is observed in heterozygotes cultured at 29–30 C throughout development. Furthermore, heterozygotes have wild-type eyes upon emergence provided development proceeds at 25 C during either of two critical periods: 1) The third quarter of the 3rd larval instar or 2) an imprecisely defined pupal period beginning less than 12 hours before the visual appearance of brown eye pigment and terminating about the time pigment appears in the wings.     

Isolation and Characterization of Rifampin-Resistant and Streptolydigin-Resistant Mutants of Bacillus subtilis with Altered Sporulation Properties

Mutants of Bacillus subtilis with altered deoxyribonucleic-dependent ribonucleic acid polymerase activity have been isolated and characterized. These mutants, selected as strains resistant to rifampin or streptolydigin, demonstrate drug-resistant in vitro ribonucleic acid synthesis. Sporeforming ability and support of phage infection are altered in many of the mutants. Mutations to rifampin and streptolydigin resistance have been located on the B. subtilis chromosome and ordered relative to the markers cysA14 and str.     

Dosage Compensation of Genes on the Left and Right Arms of the X Chromosome of DROSOPHILA PSEUDOOBSCURA and DROSOPHILA WILLISTONI

We have investigated the occurrence of dosage compensation in D. willistoni and D. pseudoobscura, two species whose X chromosome is metacentric with one arm homologous to the X and the other homologous to the left arm of chromosome 3 of D. melanogaster. Crude extracts were assayed for isocitrate dehydrogenase (XR), glucose-6-phosphate dehydrogenase (XL?), 6-phosphogluconate dehydrogenase (XL?), and α-glycerophosphate dehydrogenase (chromosome 2) in D. willistoni, and for esterase-5 (XR), glucose-6-phosphate dehydrogenase (XL?), 6-phosphogluconate dehydrogenase (XL?) and amylase (chromosome 3) in D. pseudoobscura. Our results indicate that a mechanism for dosage compensation is operative in both arms of the X chromosome of these two species.     

Attraction and attachment of zoospores of the parasitic chytridRozella allomycis in response to host-dependent factors

Summary This study examined the behavior of populations of zoospores of the obligately parasitic, endobiotic chytridRozella allomycis towards young, vegetative thalli of various saprophytic fungi, in order to identify host-dependent factors which control the development ofRozella. An inverted microscope was employed for continuous observation of parasite-host interaction in petri dishes of broth or agar medium. Two factors appear to control the initial stages of invasion byRozella of both susceptible and resistant species of the host genus,Allomyces: (i) a soluble exudate which attractsRozella zoospores, (ii) a receptor on the cell-wall surface which causesRozella zoospores to adhere, and to encyst and to germinate immediately thereafter. A related, nonsusceptible species,Blastocladiella emersonii, also attractsRozella zoospores, but supports very limited attachment.Rozella zoospores neither accumulate around, nor adhere to young thalli of non-blastocladialean fungi. This host-specific behavior pattern is compared with that of saprophytic and facultatively parasitic Phycomycetes, whose zoospores show nonspecific chemotactic responses and require no receptor for attachment, encystment and germination.     

Metal cofactor requirement of β-lactamase II

1. The apoenzyme obtained on removal of Zn(2+) from beta-lactamase II from Bacillus cereus 569/H/9 showed less than 0.001% of the activity of the Zn(2+)-containing enzyme. 2. Removal of Zn(2+) led to a conformational change in the enzyme and partial unmasking of a thiol group. 3. Replacement of Zn(2+) by Co(2+), Cd(2+), Mn(2+) or Hg(2+) gave enzymes with significant, but lower, beta-lactamase activity. No activity was detected in the presence of Cu(2+), Ni(2+), Mg(2+) or Ca(2+). 4. Equilibrium dialysis indicated that the enzyme had at least two Zn(2+) binding sites. With benzylpenicillin as substrate the variation in activity with concentration of Zn(2+) indicated that activity paralleled binding of Zn(2+) to the site of highest affinity. 5. Replacement of Zn(2+) by Co(2+) and Cd(2+) gave enzymes with absorption bands at 340 and 245nm respectively, and raised the question of whether the thiol group in the enzyme is a metal-ion ligand. 6. Reduction of the product obtained by reaction of denatured beta-lactamase II with Ellman's reagent [5,5'-dithiobis-(2-nitrobenzoic acid)] gave a protein which could refold to produce beta-lactamase II activity in high yield.     

Conformational changes in the extracellular β-lactamase I from Bacillus cereus 569/H/9

1. The thermal denaturation and precipitation of beta-lactamase I from Bacillus cereus 569/H/9 at 60 degrees C are reversible, a soluble and almost fully active enzyme being obtained after solution of the precipitate in 5m-guanidinium chloride or 8m-urea and subsequent removal of the denaturing agent. 2. Inactivation of beta-lactamase I occurs rapidly between 50 degrees and 55 degrees C and is shown by circular-dichroism spectra to be accompanied by an extensive conformational change. 3. A change to a different conformation occurs in 6m-urea. This change is also reversible; refolding with almost complete recovery of enzymic activity occurs within 5min of dilution of the denaturing agent. 4. Inactivation of beta-lactamase I at pH3.0 and 11.0 is also associated with conformational changes, since a proportion of the lost activity is recovered within 5min of adjustment of the pH to 7.0.