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PubMed1976

Genetic control of immune response against random copolymers of glutamic acid and alanine (GA) and tyrosine (GT) in inbred mice.

An immune response (lr) gene(s) controlling responses to synthetic random copolymers of two amino acids of glutamic acid and alanine (GA) in mice has been well documented. This specific lr gene is linked to the major histocompatibility complex of the species. Mice of the H-2a,b,d,f,k,r and s haplotypes produce high titer antibodies and thus are high responders; whereas mice of the H-2 haplotypes j, ja, p and q produce no detectable antibody and are non responders. The response is "all or none" and high response is dominant. Attempts to detect an Ir-GT gene (glutamic acid and tyrosine) after immunization with two GT random copolymers were unsuccessful. However, GT-antibody could be produced after immunization with GT-methylated bovine serum albumin aggregates.

Alanine↗
PubMed2000

Proton translocation by cytochrome c oxidase can take place without the conserved glutamic acid in subunit I.

A glutamic acid residue in subunit I of the heme-copper oxidases is highly conserved and has been directly implicated in the O(2) reduction and proton-pumping mechanisms of these respiratory enzymes. Its mutation to residues other than aspartic acid dramatically inhibits activity, and proton translocation is lost. However, this glutamic acid is replaced by a nonacidic residue in some structurally distant members of the heme-copper oxidases, which have a tyrosine residue in the vicinity. Here, using cytochrome c oxidase from Paracoccus denitrificans, we show that replacement of the glutamic acid and a conserved glycine nearby lowers the catalytic activity to <0.1% of the wild-type value. But if, in addition, a phenylalanine that lies close in the structure is changed to tyrosine, the activity rises more than 100-fold and proton translocation is restored. Molecular dynamics simulations suggest that the tyrosine can support a transient array of water molecules that may be essential for proton transfer in the heme-copper oxidases. Surprisingly, the glutamic acid is thus not indispensable, which puts important constraints on the catalytic mechanism of these enzymes.

Amino Acid Sequence↗
PubMed1983

Excitatory effect of intrahippocampal injection of glutamic acid on rabbit EEG.

Glutamic acid microinjection into the rabbit dorsal hippocampus was studied in its effects on hippocampal and cortical electroencephalogram (EEG). The studies were carried out on rabbits with chronically implanted electrodes and cannulae. Bipolar, silver recording electrodes and stainless steel cannulae were implanted into the hippocampus, and recording electrodes were placed on the surface of the frontal and cingular cortical areas. Low doses of glutamic acid (5-25 nM) induced EEG and behavioral arousal. Short lasting epileptiform-like seizures and behavioral convulsions were induced after injection of high doses of glutamic acid (100-500 nM). These findings suggest that glutamic acid in the hippocampus of the rabbit is involved in behavioral arousal and epileptiform-like disorders.

Animals↗
PubMed1983

Reconstitution mechanism of nucleosome core particles mediated by poly(L-glutamic acid).

Poly(L-glutamic acid) has been reported to mediate in vitro nucleosome assembly (Stein, A., Whitlock, J.P., Jr. and Bina, M. (1979) Proc. Natl. Acad. Sci. U.S.A. 76,5000-5004). To study the reaction mechanism, we have reconstituted nucleosome core particles from chicken erythrocyte core DNA and core histones in the presence of poly(L-glutamic acid) and analyzed the assembly products by polyacrylamide gel electrophoresis. Poly(L-glutamic acid), which binds and forms a large complex with core histones, is replaced with core DNA in the reconstitution process. When histone-poly(L-glutamic acid) complex and core DNA are mixed with a histone:DNA ratio of 1.0, the yield of core particles increases by prolonged reconstitution time. Two phases with a distinct time range appear in the process. In the fast phase within 30 min, 60% of the DNA is involved in products containing histones: reconstituted core particles, a larger nucleoprotein complex and aggregation. In the second phase, the remaining DNA and the DNA in the aggregation decrease, and the core particles increase slowly. The yield of core particles is approx. 60% after 24 h. The slow phase is not observed by reconstitution with a histone:DNA ratio of 2.0 in the initial mixture. The reaction scheme of the assembly process derived from these data is given. Based on the in vitro reaction scheme, the possible role of in vivo 'nucleosome assembly factors' is also discussed.

Animals↗