Superprecipitation-Like Phenomenon and Destruction Induced by Adenosine 5′-Triphosphate in Spirosomes Isolated from Lactobacillus brevis

• Published in: Microbiology and immunology Vol. 26; no. 10; pp. 979 - 983
• Main Authors: Kawata, Tomio, Masuda, Kuniyoshi, Nomura, Shuichi
• Format: Journal Article
• Language: English
• Published: Australia Blackwell Publishing Ltd 01.10.1982
• Subjects: Acholeplasma; Adenosine Triphosphate - pharmacology; Bacterial Proteins - isolation & purification; Cell Fractionation; Clostridium; Escherichia coli; Inclusion Bodies - drug effects; Lactobacillus - analysis; Lactobacillus - ultrastructure; Lactobacillus brevis; Protein Conformation - drug effects
• ISSN: 0385-5600; 1348-0421
• DOI: 10.1111/j.1348-0421.1982.tb00245.x

The authors detected very fine spirals in membrane fractions of L. fermentum and L. casei and called them spirosomes on the basis of their morphological characteristics. Later, They isolated spirosomes from protoplasts of L. brevis and examined their ultrastructure under the electron microscope. The spirosomes consist of a left-handed helical structure about 6.5 nm in width, 12.5 nm in height and 11 nm in pitch, and its length ranges from 30 to 900 nm with a high frequency of 100 to 200 nm. Spirosomes or similar spiral inclusions have been widely found in gram-positive and -negative bacteria. The spirosome sensitive to proteolytic digestion is composed of a single protein, termed spirosin, with an apparent molecular weight of about 95,000 as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. A similar cytoplasmic helical structure was isolated from Acholeplasma laidlawii and was found to be composed of a predominant polypeptide with a molecular weight of 100,000. The authors found that spirosomes purified from L. brevis are superprecipitated as in the case of actomyosin and morphologically destroyed immediately after addition of adenosine 5'-triphosphate (ATP).