Response to pH shift of Rhizobium tropici CIAT 899 and Rhizobium etli CIAT
611, reacting differently to reduced pH in their nodulation efficiency, was
studied by two-dimensional gel electrophoretic analysis of soluble protein
s from cells labeled with [S-35]methionine. After a pH shift from pH 6.8 to
5.2, the electrophoretic patterns of both strains revealed marked differen
ces of protein synthesis. In R. tropici CIAT 899, five polypeptides were in
creased, whereas four others were decreased in their synthesis following a
pH shift, while in R. etli CIAT 611, ten polypeptides, distinct from those
in R. tropici 899, were increased relative to pH 6.8, and the synthesis of
eight polypeptides decreased after the shift. Two pH shift induced proteins
(PipA and PipB) of R. tropici CIAT 899 were excised from two-dimensional g
els and were subjected to microsequencing, revealing similarity of PipA to
enzymes likely to be involved in the synthesis of exopolysaccharides (EPS).
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