2641 Yamazaki, Noda-shi, Chiba-ken 278-8510, Tokyo
Japan
Research Article
Detection of Key Residues Involving Functional Divergence into the Translation Elongation Factor Tu/1A Family Using Quantitative
Measurements for Specific Conservation of Protein Subfamilies
Author(s): Yosuke KondoYosuke Kondo
Delivery of an aminoacyl-tRNA to the ribosomal A-site during protein biosynthesis is mediated by elongation factor Tu/1A (EF-Tu/1A). This function is inferred as a common function of the EF-Tu/1A family. Moonlighting functions and several functional divergences are speculated in the EF-Tu/1A molecules such as actin and fibronectin binding functions. Two variant eEF1A forms, referred to as eEF1A1 and eEF1A2, are surmised to have different actin binding affinities. Mycoplasma pneumoniae EF-Tu has higher fibronectin binding affinity than M. genitalium EF-Tu. Incidentally; quantitative description for specific conservation of protein subfamilies could be helpful for assessment of the functional differences. Our paper defines two types of variability measurements of a multiple sequence alignment site. One is based upon a substitution matrix and sequence weights.. Read More»
DOI:
10.4172/jcsb.1000138
Journal of Computer Science & Systems Biology received 2279 citations as per Google Scholar report