Chimeric dihydrofolate reductases display properties of modularity and biophysical diversity.

ABSTRACT: While reverse genetics and functional genomics have long affirmed the role of individual mutations in determining protein function, there have been fewer studies addressing how large-scale changes in protein sequences, such as in entire modular segments, influence protein function and evolution. Given how recombination can reassort protein sequences, these types of changes may play an underappreciated role in how novel protein functions evolve in nature. Such studies could aid our understanding of whether certain organismal phenotypes related to protein function-such as growth in the presence or absence of an antibiotic-are robust with respect to the identity of certain modular segments. In this study, we combine molecular genetics with biochemical and biophysical methods to gain a better

SUBMITTER: Rodrigues JV 

PROVIDER: S-EPMC7663999 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature