title: TPR repeats and ELTR pattern: length variation as a function evolution mechanism.
abstract: TPR repeat was originally defined as a 34 amino acid structural repeat (TPR-34). Equal length tandem repeats (ELTR) was proposed to represent the ancestral repeat pattern. Length polymorphism of TPR repeats was analyzed using PATTINPROT, two new versions of TPR repeat of 40 and 42 amino acids were identified. These 'long' TPRs endow new functional capacities to the resulting proteins. A strong correlation between varied lengths and new functions supports the hypothesis that length variation is an underlying mechanism for the function evolution of repeat containing proteins.
authors.affiliation: State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China. yangkq@im.ac.cn
authors.forename: Ke-Qian
authors.initials: KQ
authors.lastname: Yang
mesh_terms: D000595:Amino Acid Sequence; D019143:Evolution, Molecular; D008969:Molecular Sequence Data; D028861:Nuclear Pore Complex Proteins; D011518:Proto-Oncogene Proteins; D020449:Repetitive Sequences, Amino Acid; D020080:Tandem Repeat Sequences
chemical_list: D028861:Nuclear Pore Complex Proteins; D011518:Proto-Oncogene Proteins; C073597:TPR protein, human