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Recombinant protein secretion in Escherichia coli
Biotechnology Advances, 2005The secretory production of recombinant proteins by the Gram-negative bacterium Escherichia coli has several advantages over intracellular production as inclusion bodies. In most cases, targeting protein to the periplasmic space or to the culture medium facilitates downstream processing, folding, and in vivo stability, enabling the production of ...
F J M, Mergulhão +2 more
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[Protein kinase activity in Escherichia coli].
Comptes rendus des seances de l'Academie des sciences. Serie D, Sciences naturelles, 1979When growing E. coli in a minimal medium, at least four proteins from the soluble fraction and one ribosome-associated protein are found phosphorylated at the level of their threonine and serine residues.
Manai, M., Cozzone, A.
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The stoichiometry of the ribosomal proteins of Escherichia coli
Molecular and General Genetics MGG, 1975A ribosome preparation from E. coli made without stringent washing procedures has been shown to contain the same relative amounts of nearly all the ribosomal proteins as ribosomes in intact cells. Stoichiometric measurements on all the proteins of this preparation except for L8, L20, L31 and L34 have been made using an isotope dilution technique.
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DNA Replication Proteins of Escherichia Coli
Annual Review of Biochemistry, 1978PERSPECTIVES AND SUMMARY ..... .. .. 1163 ESCHERICHIA COLI CHROMOSOME REPLICATION ........ .. ..... ...... .... 116S In Vivo DNA Replication 1165 In Vitro DNA Replication 1166 SINGLE-STRANDED CIRCULAR DNA-DEPENDENT DNA SYNTHESIS .... 1168 Priming of Single-Stranded DNA Synthesis ..
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Recombinant protein expression in Escherichia coli
Current Opinion in Biotechnology, 1999Escherichia coli is one of the most widely used hosts for the production of heterologous proteins and its genetics are far better characterized than those of any other microorganism. Recent progress in the fundamental understanding of transcription, translation, and protein folding in E.
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Heterogeneity of protein turnover in Escherichia coli
Biochimica et Biophysica Acta (BBA) - General Subjects, 1965Abstract An investigation has been made to determine the extent of turnover synthesis in the subcellular components of resting cells of Escherichia coli , and the extent to which this synthesis differs from that in normal growth. Estimates of turnover vary with the strain of organism examined, the condition of starvation and the amino acid used as ...
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Ribosomal protein synthesis by a mutant of Escherichia coli
European Journal of Biochemistry, 1984The mutant strain of Escherichia coli, TP28, synthesises ribosomes by an abnormal pathway and accumulates large quantities of 47S ribonucleoprotein particles. The protein complement of mutant 70S ribosomes is normal but 47S particles contain only traces of proteins L28 and L33 and have a significantly reduced content of four other proteins.
P D, Butler, D G, Wild
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Production of human tetraspanin proteins in Escherichia coli
Protein Expression and Purification, 2012Tetraspanins are found in multicellular eukaryotes and are generally thought to act as scaffolding proteins, localizing multiple proteins to a specific region of the cell membrane. Activities for tetraspanins have been identified in several fundamental processes such as motility, cell adhesion, proliferation and viral entry.
Michael Tarry +4 more
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Escherichia coli Repressor Proteins
1989Genetic regulation is an essential function in all living organisms. In prokaryotes genetic control provides responsivity to a constantly changing external milieu, and bacterial systems have proved extremely valuable in elucidating the variety of potential mechanisms.
Kyle L. Wick, Kathleen S. Matthews
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Protein translocation in Escherichia coli
Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1994R A, Arkowitz, M, Bassilana
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