Intron positions correlate with module boundaries in ancient proteins.

ABSTRACT: We analyze the three-dimensional structure of proteins by a computer program that finds regions of sequence that contain module boundaries, defining a module as a segment of polypeptide chain bounded in space by a specific given distance. The program defines a set of "linker regions" that have the property that if an intron were to be placed into each linker region, the protein would be dissected into a set of modules all less than the specified diameter. We test a set of 32 proteins, all of ancient origin, and a corresponding set of 570 intron positions, to ask if there is a statistically significant excess of intron positions within the linker regions. For 28-A modules, a standard size used historically, we find such an excess, with P < 0.003. This correlation is neither due to a composi

SUBMITTER: de Souza SJ 

PROVIDER: S-EPMC26186 | biostudies-literature | 1996 Dec

REPOSITORIES: biostudies-literature