Protein synthesis and degradation in a leucine auxotroph of Escherichia coli.

AUTOR(ES)

Aguanno, J J

RESUMO

The synthesis and degradation of the soluble and sodium dodecyl sulfate-(SDS)-solubilized protein fractions of Escherichia coli were studied in both growing and nongrowing cultures. When separated according to molecular weight on SDS-polyacrylamide gels, the proteins of both fractions of growing cells undergo no measureable differential synthesis or degradation during logarithmic growth. However, when a leucine auxotroph is suspended in medium containing 5.3 muM leucine (a level that will not sustain growth), the SDS-solubilized protein of such a nongrowing culture shows a rapid synthesis of two protein components (32,000 and 12,000 daltons) found only in the out membrane.

Documentos Relacionados

• Synthesis and degradation of nitrate reductase in Escherichia coli.
• Ribosomal distribution in a polyamine auxotroph of Escherichia coli.
• The leucine-responsive regulatory protein, a global regulator of metabolism in Escherichia coli.
• Immunocytological investigation of protein synthesis in Escherichia coli.
• Energy-dependent degradation of lambda O protein in Escherichia coli.