AMINO ACID INCORPORATION IN THE SUBCELLULAR STRUCTURES OF PSEUDOMONAS FLUORESCENS A3-12

II. RIBONUCLEOPROTEIN PARTICLES DERIVED FROM THE INSOLUBLE STRUCTURES OF BACTERIA AND THE INCORPORATION OF S³⁵-METHIONINE INTO "BROKEN PROTOPLAST"

Abstract

In order to understand the presence of the ribonucleoprotein particles (RNP) bound to the cytoplasmic membrane ("ghost") of Pseudomonas fluorescens A3-12, ultracentrifugal separation was applied to the disintegrated ghosts.
The release of RNP from the membranous structures into the cytoplasm during the preparation of ghosts was quantitatively studied, and the relationship between the magnitude of osmotical lysis in protoplasts and the incorporation of the "broken protoplast" for S³⁵-methionine were investigated.
It could be summarized that (1) the RNA-rich particles (RNP), regarded as the incorporation sites of amino acids, associate relatively firmly with the membranous structures preparable as the ghost, and (2) the incorporation of amino acid into a mildly broken protoplast is more prominent than that vigorously disrupted.
With reference to the results obtained in the previous paper⁽¹⁹⁾, it can be concluded that the bacterial membranous-structures are the incorporation site of amino acids and which plays an important role in protein synthesis.