Search

The DNA-binding HU-type proteins from several species of Rhizobiaceae including Rhizobium meliloti, two strains of Rhizobium leguminosarum with highly different phenotypic characters and Agrobacterium tumefaciens, were characterized and their amino acid sequences were determined. HU-type proteins isolated form R. leguminosarum L18 and A. tumefaciens are identical and show slight differences with the R. meliloti HU-type protein. On the other hand the R. leguminosarum L53 HU-type protein is quite different from the proteins cited above; several amino acid substitutions encountered in this protein result bacteria in the phylogeny determined by numerical taxonomy. [ABSTRACT FROM AUTHOR]

The amino acid sequence of protein HRm, a DNA-binding HU-type protein of 90 residues (Mr 9303). isolated from Rhizobium meliloti, has been established from automated sequence analysis of the protein and from structural data provided by peptides derived from cleavage of the protein at arginine and aspartic acid residues. The comparison of the primary structure of protein HRm with that of other HU-type proteins shows that two short sequences. of 7 and 6 residues respectively, located in the median part of' the molecule, appear highly conserved and may be important in the Function of the protein. [ABSTRACT FROM AUTHOR]