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Filamentous Bacteriophage Proteins and Assembly

2018
Filamentous bacteriophages, also known as filamentous bacterial viruses or Inoviruses, have been studied extensively over the years. They are interesting paradigms in structural molecular biology and offer insight into molecular assembly, a process that remains to be fully understood.
Suzana K, Straus, Htet E, Bo
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Structural transition in a filamentous protein

Journal of Molecular Biology, 1976
The filamentous bacterial virus Pf1 exhibits two distinct fiber diffraction patterns. The transition between these patterns can best be explained by a fractional change in the number of units per turn in the coat protein helix. The stereochemistry of the transition has been examined for a detailed molecular model, and found to be energetically feasible.
E J, Wachtel, F J, Marvin, D A, Marvin
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Heterologous Protein Production by Filamentous Fungi

Biotechnology and Genetic Engineering Reviews, 1991
There are clearly many facets to successful production of heterologous proteins from filamentous fungi. The objectives are to exploit the natural ability of some species to secrete high levels of protein. The heterologous target proteins produced in a fungal host must be acceptable to the public and be economic to produce, i.e.
D J, Jeenes   +3 more
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Heterologous protein expression in filamentous fungi

Trends in Biotechnology, 2005
Filamentous fungi are commonly used in the fermentation industry for the large-scale production of proteins--mainly industrial enzymes. Recent advances in fungal genomics and related experimental technologies such as gene arrays and proteomics are rapidly changing the approaches to the development and use of filamentous fungi as hosts for the ...
K M Helena, Nevalainen   +2 more
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Protein-protein Interactoins During Filamentous Phage Assembly

Journal of Molecular Biology, 1993
Filamentous phage proteins pI and pIV are morphogenetic proteins required for phage assembly but not part of the virion. Neither pI nor pIV from the related phages f1 and IKe can substitute for its equivalent in the other phage. When the two proteins are supplied as pairs, however, partial restoration of heterologous phage assembly occurs.
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Hamiltonian Dynamics of Protein Filament Formation

Physical Review Letters, 2016
We establish the Hamiltonian structure of the rate equations describing the formation of protein filaments. We then show that this formalism provides a unified view of the behavior of a range of biological self-assembling systems as diverse as actin, prions, and amyloidogenic polypeptides.
Thomas C. T. Michaels   +4 more
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Filamentous Proteins from Plant Sieve Tubes

Nature New Biology, 1971
PROTEIN filaments are characteristic structural components of the assimilatory conducting elements of angiosperm plants (“P protein” of Cronshaw and Esau1). We have isolated filamentous structures from the phloem exudate of cut cucurbit stems2. The presence of the filaments could be clearly demonstrated after negative staining with the electron ...
H, Kleinig   +3 more
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Evolutionary aspects in intermediate filament proteins

Current Opinion in Cell Biology, 2015
Intermediate filament (IF) proteins, together with tubulins and actins, constitute the majority of cytoskeletal proteins in metazoans. Proteins of the IF family fulfil increasingly diverse functions but share common structural features. Phylogenetic analysis within the metazoan lineage traces back their origin to a common lamin-like ancestor.
Annette, Peter, Reimer, Stick
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Intermediate Filament-Associated Proteins

1990
Intermediate filaments (IF) comprise a set of ~ 10-nm-diameter cytoskeletal filaments that are distributed throughout the cytoplasm from the level of the nuclear surface to the region of the plasma membrane in most eukaryotic cells (Ishikawa et. al., 1968; Traub, 1985a; Wang et. al., 1985; Goldman et. al., 1986).
Hsi-Yuan Yang   +2 more
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Implications of intermediate filament protein phosphorylation

Cancer and Metastasis Review, 1996
Intermediate filament (IF) proteins, a large family of tissue specific proteins, undergo several posttranslational modifications, with phosphorylation being the most studied modification. IF protein phosphorylation is highly dynamic and involves the head and/or tail domains of these proteins, which are the domains that impart most of the structural ...
N O, Ku, J, Liao, C F, Chou, M B, Omary
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