T4 gene 40 mutants

Brown, Scott M.; Eiserling, Frederick A.

doi:10.1016/0042-6822(79)90374-x

Virology

1979

DOI: 10.1016/0042-6822(79)90374-x

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T4 gene 40 mutants

Scott M. Brown

Frederick A. Eiserling

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Cited by 14 publications

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Protein nanomachines assembly modes: cell‐free expression and biochip perspectives

Daube

Bar‐Ziv

2013

WIREs Nanomed Nanobiotechnol

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Large macromolecular assemblies are widespread in all cell types with diverse structural and functional roles. Whether localized to membranes, nuclei, or cytoplasm, multimeric protein-nucleic acid complexes may be viewed as sophisticated nanomachines, an inspiration to chemical design. The formation of large biological assemblies follows a complex and hierarchical self-assembly process via ordered molecular recognition events. Serving a paradigm for biological assembly, extensive past studies of T4 bacteriophage and bacterial ribosomes by many groups have been revealing distinct design strategies, yet these two very different multimeric complexes share common mechanistic motifs. An emerging biochip approach highlights two conceptual notions to promote the study of assembly pathways: cell-free expression provides coupling between synthesis and assembly; surface anchoring allows high-resolution imaging of structural intermediates and opens up opportunities for rewiring a network by defining unnatural scaffolds for synthetic design applications.

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Protein nanomachines assembly modes: cell‐free expression and biochip perspectives

Daube

Bar‐Ziv

2013

WIREs Nanomed Nanobiotechnol

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The Structural Protein E of the Archaeal Virus φCh1: Evidence for Processing in Natrialba magadii during Virus Maturation

et al. 2000

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phiCh1 is a lysogenic virus for the haloalkalophilic archaeon Natrialba magadii. The virus morphology resembles other members of Myoviridae infecting Halobacterium species. The gene of the major capsid protein E of virus phiCh1 was cloned and the DNA sequence was determined. Gene E was mapped to a 3.2-kbp ClaI fragment, localized to the 5'-end of the phiCh1 genome. The complete nucleotide sequence of this region was determined and the identity of gene E was confirmed by comparing the experimentally determined N-terminal amino acid sequence of the purified protein to the translated DNA sequence of its open reading frame. We present evidence that the gene E product is proteolytically cleaved between Lys(16) and Asn(17) to yield the 305 residue polypeptides found in the mature viral capsid. Processing of the protein itself during virus development was determined by 2D gel electrophoresis using protein E-specific antibodies. Sequence similarity studies revealed an 80% identity to capsid protein Hp32 of phiH, infecting Halobacterium salinarum. RT-PCR analysis as well as Western blot studies revealed gene E as a late gene. Transcripts and proteins could be detected shortly before onset of lysis of the lysogenic strain N. magadii L11.

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Gene 20 product of bacteriophage T4 its purification and structure

Driedonks

Engel

tenHeggeler

et al. 1981

Journal of Molecular Biology

100

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T4 gene 40 mutants

Cited by 14 publications

References 42 publications

Protein nanomachines assembly modes: cell‐free expression and biochip perspectives

Protein nanomachines assembly modes: cell‐free expression and biochip perspectives

The Structural Protein E of the Archaeal Virus φCh1: Evidence for Processing in Natrialba magadii during Virus Maturation

Gene 20 product of bacteriophage T4 its purification and structure

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