Fibritin Encoded by Bacteriophage T4 Gene wac has a Parallel Triple-stranded α-Helical Coiled-coil Structure

Efimov, Vladimir P.; Nepluev, Igor; Sobolev, Boris N.; Zurabishvili, T.G.; Schulthess, Therese; Lustig, Ariel; Engel, Juergen; Haener, Markus; Aebi, Ueli; Venyaminov, Sergey Yu.; Potekhin, Sergey A.; Mesyanzhinov, Vadim V.

doi:10.1006/jmbi.1994.1595

Cited by 44 publications

(65 citation statements)

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“…The construction of the twostranded coiled-coil database is discussed in Berger et al The three-stranded coiled-coil database was constructed from 42 sequences. The proteins in the three-stranded database have been characterized in the following references: laminins (families A, Bl, and B2 chains) (Pikkarainen et al, 1987(Pikkarainen et al, , 1988Sasaki et al, , 1988Monte11 & Goodman, 1988Hunter et al, 1989Hunter et al, , 1992Engel, 1992;Kallunki et al, 1992;Nomizu et al, 1992;Beck et al, 1993;Porter et al, 1993;Gerecke et al, 1994;Vuolteenaho et al, 1994;Wewer et al, 1994), fibrinogens (families a, j?, and y chains) (Chung et al, 1981(Chung et al, , 1983a(Chung et al, , 1983bCrabtree & Kant, 1982;Rixon et al, 1983;Crabtree et al, 1985;Strong et al, 1985;Bohonus et al, 1986;Koyama et al, 1987;Wang et al, 1989;Pastori et al, 1990;Weissbach & Grieninger, 1990;Pan & Doolittle, 1992), K. lactis heat shock factor (Peteranderl & Nelson, 1992), S. cerevisiae heat shock transcription factor (Sorger & Nelson, 1989), influenza virus hemagglutinin (Bullough et al, 1994), Moloney murine leukemia virus ( Fass et al, 1996), fibritin encoded by Wac gene for bacteriophage T4 and K3 (Efimov et al, 1994), gp17 leg protein in bacteriophages T7 and T3, and macrophage scavenger receptor protein (Conway & Parry, 1991).…”

Section: Databases and Probability Estimatesmentioning

confidence: 99%

MultiCoil: A program for predicting two‐and three‐stranded coiled coils

Wolf

Kim

Berger³

1997

Protein Science

703

602

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A new multidimensional scoring approach for identifying and distinguishing trimeric and dimeric coiled coils is implemented in the MultiCoil program. The program extends the two-stranded coiled-coil prediction program PairCoil to the identification of three-stranded coiled coils. The computations are based upon data gathered from a three-stranded coiled-coil database comprising 6,319 amino acid residues, as well as from the previously constructed two-stranded coiled-coil database. In addition to identifying coiled coils not predicted by the two-stranded database programs, MultiCoil accurately classifies the oligomerization states of known dimeric and trimeric coiled coils. Analysis of the MultiCoil scores provides insight into structural features of coiled coils, and yields estimates that 0.9% of all protein residues form three-stranded coiled coils and that 1.5% form two-stranded coiled coils. The MultiCoil program is available at http://theory.Ics.mit.edu/multicoil.

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Section: Databases and Probability Estimatesmentioning

confidence: 99%

MultiCoil: A program for predicting two‐and three‐stranded coiled coils

Wolf

Kim

Berger³

1997

Protein Science

703

602

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“…Since the 30-aa C-terminal domain of the T4 gpwac is required for the initiation of trimerization and folding (14,23), this segment was expected to be conserved among all gpwac homologs. The C-terminal amino acid sequences of the wac gene from 13 closely related T-even phages were virtually identical to that of the T4 protein (sequence data not shown).…”

Section: Structure and Function Of The Wac Protein Of Phage T4mentioning

confidence: 99%

“…The T4 virion actually contains three sets of fibrous structures with distinct functions: the long tail fibers (LTFs), which are involved in reversible adsorption; the short tail fibers, which are involved in the final, irreversible step of adsorption; and the gpwac-encoded "collar-whiskers" (40). gpwac forms a collar (10,13) on the phage neck of six radiating 480-Å fibrils that can bind transiently to the LTFs and properly position them for attachment to the baseplate (14,15,40). These whiskers also have a potentially important regulatory function; they act as part of an environmental sensing device that prevents phage absorption in conditions unsuitable for infection (e.g., low pH).…”

mentioning

confidence: 99%

“…Both LTFs and short tail fibers have a similar trimeric parallel ␤-helical protein structure (26,39). However, the 486-amino-acid (aa) T4 gpwac polypeptide trimerizes into a coiled-coil ␣-helical structure that is flanked by small N-and C-terminal globular domains (14,28,33). It is the N-terminal 50-aa domain of T4 gpwac that binds to the neck of the phage, whereas the 30-aa C-terminal domain of the protein (the "foldon") is essential for the initiation of trimerization and the correct folding of the polypeptide chains in the fiber (14,23).…”

mentioning

confidence: 99%

“…However, the 486-amino-acid (aa) T4 gpwac polypeptide trimerizes into a coiled-coil ␣-helical structure that is flanked by small N-and C-terminal globular domains (14,28,33). It is the N-terminal 50-aa domain of T4 gpwac that binds to the neck of the phage, whereas the 30-aa C-terminal domain of the protein (the "foldon") is essential for the initiation of trimerization and the correct folding of the polypeptide chains in the fiber (14,23). The nucleotide sequences of the wac genes from a few T-even phages very closely related to T4 have been determined previously (M. M. Schneider et al, unpublished data; our unpublished results), but the amino acid sequences of all of these proteins are virtually identical to that of T4 gpwac.…”

mentioning

confidence: 99%

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gpwac of the T4-Type Bacteriophages: Structure, Function, and Evolution of a Segmented Coiled-Coil Protein That Controls Viral Infectivity

et al. 2005

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The wac gene product (gpwac) or fibritin of bacteriophage T4 forms the six fibers that radiate from the phage neck. During phage morphogenesis these whiskers bind the long tail fibers (LTFs) and facilitate their attachment to the phage baseplate. After the cell lysis, the gpwac fibers function as part of an environmental sensing device that retains the LTFs in a retracted configuration and thus prevents phage adsorption in unfavorable conditions. A comparative analysis of the sequences of 5 wac gene orthologs from various T4-type phages reveals that the ϳ50-amino-acid N-terminal domain is the only highly conserved segment of the protein. This sequence conservation is probably a direct consequence of the domain's strong and specific interactions with the neck proteins. The sequence of the central fibrous region of gpwac is highly plastic, with only the heptad periodicity of the coiled-coil structure being conserved. In the various gpwac sequences, the small C-terminal domain essential for initiation of the folding of T4 gpwac is replaced by unrelated sequences of unknown origin. When a distant T4-type phage has a novel C-terminal gpwac sequence, the phage's gp36 sequence that is located at the knee joint of the LTF invariably has a novel domain in its C terminus as well. The covariance of these two sequences is compatible with genetic data suggesting that the C termini of gpwac and gp36 engage in a protein-protein interaction that controls phage infectivity. These results add to the limited evidence for domain swapping in the evolution of phage structural proteins.

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The episodic evolution of fibritin: traces of ancient global environmental alterations may remain in the genomes of T4‐like phages

Letarov¹,

Krisch

2013

Ecology and Evolution

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The evolutionary adaptation of bacteriophages to their environment is achieved by alterations of their genomes involving a combination of both point mutations and lateral gene transfer. A phylogenetic analysis of a large set of collar fiber protein (fibritin) loci from diverse T4-like phages indicates that nearly all the modular swapping involving the C-terminal domain of this gene occurred in the distant past and has since ceased. In phage T4, this fibritin domain encodes the sequence that mediates both the attachment of the long tail fibers to the virion and also controls, in an environmentally sensitive way, the phage's ability to infect its host bacteria. Subsequent to its distant period of modular exchange, the evolution of fibritin has proceeded primarily by the slow vertical divergence mechanism. We suggest that ancient and sudden changes in the environment forced the T4-like phages to alter fibritin's mode of action or function. The genome's response to such episodes of rapid environmental change could presumably only be achieved quickly enough by employing the modular evolution mechanism. A phylogenetic analysis of the fibritin locus reveals the possible traces of such events within the T4 superfamily's genomes.

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Fibritin Encoded by Bacteriophage T4 Gene wac has a Parallel Triple-stranded α-Helical Coiled-coil Structure

Cited by 44 publications

References 0 publications

MultiCoil: A program for predicting two‐and three‐stranded coiled coils

MultiCoil: A program for predicting two‐and three‐stranded coiled coils

gpwac of the T4-Type Bacteriophages: Structure, Function, and Evolution of a Segmented Coiled-Coil Protein That Controls Viral Infectivity

The episodic evolution of fibritin: traces of ancient global environmental alterations may remain in the genomes of T4‐like phages

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