Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
The lambda spanin components Rz and Rz1 undergo tertiary and quaternary rearrangements upon complex formation.
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Equimolar mixing of the soluble periplasmic domains of Rz and Rz1 induces an unstructured-to-helical conformational rearrangement, and Rz1 binding stabilizes Rz against periplasmic proteolysis in vivo.
"The results indicate that in vivo , Rz1 protects the C-terminal domain of Rz from proteolysis by forming a complex that spans the entire periplasm through the meshwork of the intact PG."
The spanin complex is essential for lambda lysis.
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Rz1 is unconditionally required for outer membrane rupture during bacteriophage lambda host lysis.
"In both cases, lysis failed to occur in inductions of isogenic prophages carrying null mutations in the spanin genes. In both systems, instead of an envelope rupture, the induced cells were converted from a rod shape to a spherical form."
Spanin function requires subunit homodimerization through intermolecular disulfide bonds.
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Mature Rz1 is an outer membrane lipoprotein with 25% proline content that forms a covalent homodimer via an intermolecular disulfide bond at Cys-29.
"Rz, the inner membrane or i-spanin, has a largely alpha-helical periplasmic domain, whereas Rz1, the outer membrane or o-spanin, has a 25% proline content with no predicted secondary structure."
Membrane fusion during phage lysis.
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The lambda Rz-Rz1 spanin complex mediates fusion of the Escherichia coli inner and outer membranes as the terminal step of phage lysis.
"Here we show that the spanins of the paradigm coliphage lambda mediate efficient membrane fusion. This supports the notion that the last step of lysis is the fusion of the IM and OM."
Genetic Analysis of the Lambda Spanins Rz and Rz1: Identification of Functional Domains.
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Genetic dissection of Rz and Rz1 defines the C-terminal interaction determinants and central proline-rich region of Rz1 required for outer membrane disruption.
"Coliphage lambda proteins Rz and Rz1 are the inner membrane and outer membrane subunits of the spanin complex-a heterotetramer that bridges the periplasm and is essential for the disruption of the outer membrane during phage lysis."
The Rz1 gene product of bacteriophage lambda is a lipoprotein localized in the outer membrane of Escherichia coli.
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Rz1 is processed by signal peptidase II into a lipoprotein that localizes almost exclusively to the Escherichia coli outer membrane.
"In induced Escherichia coli lambda lysogens Rz1 was found almost exclusively in the outer membrane (OM)."