INTEREST GROUPS AND LITIGATION
Interest groups engaged in litigation are faced with questions of litigation strategy and of allocation of resources. Planned constitutional litigation, part of mobilization of the law, is problematic, as is the choice of forum in which the litigation is brought. Litigation by interest groups is affected by the political environment, including judicial rulings; the complexity of litigation itself; inter-organizational relations; and, most importantly, a series of intra-organizational factors. The latter include control of litigation, group longevity, relations between lawyers and organization, and organizational structure. These elements of interest group litigation are explored in this article.
The South Counterattacks: the Anti-Naacp Laws
N RECENT YEARS the group basis of judicial activity has become more evident. Whether this has been due to heavier group pressures or whether there has simply been sharper recognition of what has always been going on, is difficult to determine.' Perhaps the current situation is partially the result of both factors. Certainly the dispute over national economic policy during the depression years, when the foes of the New Deal took their lost political cause to the judges, focused attention on judicial pressure groups. Organized labor profited by this example; and in the decade after 1937, when the liberalism of the Roosevelt coalition was in legislative eclipse, unions found their staunchest support in the marble palace across the street from the capitol building. As a concomitant of this economic battle public awareness of the immense policy potential of new judicial appointments increased, although aside from the famous Court packing plan of 1937 it is problematical whether partisan activity grew in the same proportion. There are a number of court weapons ready at hand for interest groups. The most obvious is to persuade an individual or a company to violate a law and force the government to bring a test prosecution. The amicus curiae brief2 is more oblique as well as less risky, though it normally depends on somebody else's starting the legal action. Where a plaintiff can be found a "class action" 3 for a declaratory judgment and/or an injunction can be begun, that is, a suit initiated by one person or a small group of persons on behalf of a large number of people "similarly situated."
A single amino acid substitution in elongation factor Tu disrupts interaction between the ternary complex and the ribosome
Elongation factor Tu (EF-Tu).GTP has the primary function of promoting the efficient and correct interaction of aminoacyl-tRNA with the ribosome. Very little is known about the elements in EF-Tu involved in this interaction. We describe a mutant form of EF-Tu, isolated in Salmonella typhimurium, that causes a severe defect in the interaction of the ternary complex with the ribosome. The mutation causes the substitution of Val for Gly-280 in domain II of EF-Tu. The in vivo growth and translation phenotypes of strains harboring this mutation are indistinguishable from those of strains in which the same tuf gene is insertionally inactivated. Viable cells are not obtained when the other tuf gene is inactivated, showing that the mutant EF-Tu alone cannot support cell growth. We have confirmed, by partial protein sequencing, that the mutant EF-Tu is present in the cells. In vitro analysis of the natural mixture of wild-type and mutant EF-Tu allows us to identify the major defect of this mutant. Our data shows that the EF-Tu is homogeneous and competent with respect to guanine nucleotide binding and exchange, stimulation of nucleotide exchange by EF-Ts, and ternary complex formation with aminoacyl-tRNA. However various measures of translational efficiency show a significant reduction, which is associated with a defective interaction between the ribosome and the mutant EF-Tu.GTP.aminoacyl-tRNA complex. In addition, the antibiotic kirromycin, which blocks translation by binding EF-Tu on the ribosome, fails to do so with this mutant EF-Tu, although it does form a complex with EF-Tu. Our results suggest that this region of domain II in EF-Tu has an important function and influences the binding of the ternary complex to the codon-programmed ribosome during protein synthesis. Models involving either a direct or an indirect effect of the mutation are discussed.