Arthrobacter globiformis and a Pseudomonas soil isolate were incubated separately and in combination in soil that had been presterilized by autoclaving. Growth and other responses of the cells in situ in this soil were monitored by plate counts and transmission electron microscopy examinations of cell sections. During the soil incubations, some of the samples were first allowed to dry and then were remoistened with water or with a dilute or a concentrated nutrient solution. Based on plate counts and ultrastructural analyses, Arthrobacter seemed to be in a non-multiplying coccoid-rod resting state and to be virtually immune to soil drying. Addition of a dilute nutrient solution helped maintain cell ultrastructure and prevent a low level of lysing that occurred in the absence of nutrient addition. Addition of a concentrated nutrient solution brought on cell multiplication as both coccoid-rods and long rods, but the ultimate form with further incubation was the coccoid-rod. The Pseudomonas strain suffered death and ultrastructural deterioration as water became less available. It responded by cell multiplication to an equal extent when either water or dilute nutrients were added, but possibly was able to give a growth response to nutritive amendment when a concentrated nutrient addition was made. The Arthrobacter was not affected by the presence ofPseudomonas in dual culture. The Pseudomonas, however, possibly suffered a nutritive deficiency under these conditions.

Enolase is involved in the glycolytic pathway of many organisms and is a key rate-limiting enzyme, which plays an important role in the growth and development of various species. In this study, the enolase gene sequences and amino acid sequences of more than 40 species were first downloaded, and phylogenetic analysis and molecular evolution studies were performed using bioinformatics methods. The phylogenetic tree was constructed to predict the conserved type of enolase evolution and the enolase evolution relationship of each species. It was found that the enolase of each species was very conservative during the evolution process. In addition to studying the evolutionary relationship of enolase of various species, the protein structure was predicted, and the secondary structure of enolase protein was predicted. The results showed that the secondary structure was very similar. The homology modeling method was used to predict the tertiary structure of enolase, and it was found that although there were slight differences, they were similar. In addition, statistical comparison analysis of the introns of each species enolase found that the gap between the number of introns and the locus was small, suggesting their close evolutionary relationship. It is predicted that a variety of plant and animal enolase catalytic kinasespecific phosphorylation sites, the results show that the kinase domain sequence contains three phosphorylation sites: serine (Ser), threonine (Thr) and tyrosine (Tyr). The amount of serine is the highest and the degree of similarity is high. The Ka/Ks ratio of most species is greater than 1. This indicates that enolase is mainly influenced by positive selection in evolution. Our results will help provide insights into the evolution of enolase and provide a theoretical basis for subsequent experiments.