Mutations in Gene lamB : Studies on Structure and Topology of an E. coli Outer Membrane Protein(MEMBRANE PROTEINS AND TRANSPORT-II)
スポンサーリンク
概要
- 論文の詳細を見る
Results obtained in E. coli with a set of mutations confering tight resistance to phage λ lead to a first identification of three residues in the lamB protein which are important for adsorption of phage λ. Residues 151 and 382 are important for reversible adsorption while residue 401 is important for irreversible adsorption. The identification of such residues may help to identify portions of the protein located at the cell surface. Assays of λ receptor activity in merodiploid strains heterogenote for gene lamB show that the mutations studied can have a negative dominant effect. For one class of mutations (class II) this can be interpreted by negative complementation at the level of oligomerisation. The data confirm then that active λ receptor is a trimer.
- 東海大学の論文
- 1982-06-14
著者
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Marchal Christian
Unite De Programmation Moleculaire Et Toxicologie Genetique Institut Pasteur
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Hofnung Maurice
Unite De Programmation Moleculaire Et Toxicologie Genetique Institut Pasteur
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CLEMENT Jean
Unite de Programmation Moleculaire et Toxicologie Genetique, institut pasteur
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Clement Jean
Unite De Programmation Moleculaire Et Toxicologie Genetique Institut Pasteur
関連論文
- Overcoming the crypticity of a viral T cell determinant by insertion into a chimeric bacterial protein
- Mutations in Gene lamB : Studies on Structure and Topology of an E. coli Outer Membrane Protein(MEMBRANE PROTEINS AND TRANSPORT-II)