Structure of bacteriophage T4 genes 37 and 38

Beckendorf, Steven K.; Kim, Jung Suh; Lielausis, I.

doi:10.1016/0022-2836(73)90156-3

Cited by 54 publications

(14 citation statements)

References 20 publications

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“…Phages of the T4 family recognize their cellular receptor (outer membrane protein C or LPS) using the C-terminus of the distal long tail fiber protein encoded by gp37 T4 -like protein4142. The distal long tail fiber protein ORF241 SH7 differs from gp37 T4 , sharing only 37% identity, mostly located at the N-terminus of this protein.…”

Section: Resultsmentioning

confidence: 99%

Characterization of two polyvalent phages infecting Enterobacteriaceae

Hamdi

Rousseau²,

Labrie³

et al. 2017

Sci Rep

115

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Bacteriophages display remarkable genetic diversity and host specificity. In this study, we explore phages infecting bacterial strains of the Enterobacteriaceae family because of their ability to infect related but distinct hosts. We isolated and characterized two novel virulent phages, SH6 and SH7, using a strain of Shigella flexneri as host bacterium. Morphological and genomic analyses revealed that phage SH6 belongs to the T1virus genus of the Siphoviridae family. Conversely, phage SH7 was classified in the T4virus genus of the Myoviridae family. Phage SH6 had a short latent period of 16 min and a burst size of 103 ± 16 PFU/infected cell while the phage SH7 latent period was 23 min with a much lower burst size of 26 ± 5 PFU/infected cell. Moreover, phage SH6 was sensitive to acidic conditions (pH < 5) while phage SH7 was stable from pH 3 to 11 for 1 hour. Of the 35 bacterial strains tested, SH6 infected its S. flexneri host strain and 8 strains of E. coli. Phage SH7 lysed additionally strains of E. coli O157:H7, Salmonella Paratyphi, and Shigella dysenteriae. The broader host ranges of these two phages as well as their microbiological properties suggest that they may be useful for controlling bacterial populations.

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Section: Resultsmentioning

confidence: 99%

Characterization of two polyvalent phages infecting Enterobacteriaceae

Hamdi

Rousseau²,

Labrie³

et al. 2017

Sci Rep

115

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“…ORF 401, ORF 314, and ORF 194 could be cotranscribed with the late genes from the PR' promoter (22,41). Two of these genes show similarities to the tail fiber genes of T4 (32,63): ORF 314 is similar to the 3' portion of T4 gene 37, which encodes the distal portion of the T4 tail fiber (2,3,70), and ORF 194 is similar to T4 gene 38, which encodes a protein involved in the assembly of the tail fibers (66,85). Occasionally, side tail fibers are observed in electron micrographs of A virions (52); because of the similarity of ORF 314 to T4 37, it has been suggested that ORF 314 protein is incorporated into these side tail fibers (63).…”

Section: Resultsmentioning

confidence: 99%

“…Assembly of the tail fiber requires the product of gene 38, which acts as an accessory protein and is not incorporated into the virion (25,66,85,94). The host range of the T4-like phages is determined by the carboxy-terminal portion of gp37 (2,3,64).…”

Section: Resultsmentioning

confidence: 99%

“…The T-even phages are closely related, but they can be divided into two groups based on the structure of their tail fibers. In phages similar to T4, including TuIa and TuIb, the distal part of the tail fiber consists of a parallel dimer of the product of gene 37 (2,3,86). Assembly of the tail fiber requires the product of gene 38, which acts as an accessory protein and is not incorporated into the virion (25,66,85,94).…”

Section: Resultsmentioning

confidence: 99%

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DNA sequences of the tail fiber genes of bacteriophage P2: evidence for horizontal transfer of tail fiber genes among unrelated bacteriophages

1992

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We have determined the DNA sequence of the bacteriophage P2 tail genes G and H, which code for polypeptides of 175 and 669 residues, respectively. Gene H probably codes for the distal part of the P2 tail fiber, since the deduced sequence of its product contains regions similar to tail fiber proteins from phages Mu, P1, lambda, K3, and T2. The similarities of the carboxy-terminal portions of the P2, Mu, ann P1 tail fiber proteins may explain the observation that these phages in general have the same host range. The P2 H gene product is similar to the products of both lambda open reading frame (ORF) 401 (stf, side tail fiber) and its downstream ORF, ORF 314. If 1 bp is inserted near the end of ORF 401, this reading frame becomes fused with ORF 314, creating an ORF that may represent the complete stf gene that encodes a 774-amino-acid-long side tail fiber protein. Thus, a frameshift mutation seems to be present in the common laboratory strain of lambda. Gene G of P2 probably codes for a protein required for assembly of the tail fibers of the virion. The entire G gene product is very similar to the products of genes U and U' of phage Mu; a region of these proteins is also found in the tail fiber assembly proteins of phages TuIa, TuIb, T4, and lambda. The similarities in the tail fiber genes of phages of different families provide evidence that illegitimate recombination occurs at previously unappreciated levels and that phages are taking advantage of the gene pool available to them to alter their host ranges under selective pressures.

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“…Receptors at the bacterial cell surface are recognized by phage T4 with the free ends of its long tail fibers (1,26,51). These fibers consist of four proteins: p34, p35, p36, and p37.…”

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confidence: 99%

Characterization of the helper proteins for the assembly of tail fibers of coliphages T4 and lambda

et al. 1996

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Assembly of tail fibers of coliphage T4 requires the action of helper proteins. In the absence of one of these, protein 38 (p38), p37, constituting the distal part of the long tail fiber, fails to oligomerize. In the absence of the other, p57, p34 (another component of the long tail fiber), p37, and p12 (the subunit of the short tail fiber) remain unassembled. p38 can be replaced by the Tfa (tail fiber assembly) protein (pTfa) of phage , which has the advantage of remaining soluble even when produced in massive amounts. The mechanisms of action of the helpers are unknown. As a first step towards elucidation of these mechanisms, p57 and pTfa have been purified to homogeneity and have been crystallized. The identity of gene 57 (g57), not known with certainty previously, has been established. The 79-residue protein p57 represents a very exotic polypeptide. It is oligomeric and acidic (an excess of nine negative charges). It does not contain Phe, Trp, Tyr, His, Pro, and Cys. Only 25 N-terminal residues were still able to complement a g57 amber mutant, although with a reduced efficiency. In cells overproducing the protein, it assumed a quasi-crystalline structure in the form of highly ordered fibers. They traversed the cells longitudinally (and thus blocked cell division) with a diameter approaching that of the cell and with a hexagonal appearance. The 194-residue pTfa is also acidic (an excess of 13 negative charges) and is likely to be dimeric.Receptors at the bacterial cell surface are recognized by phage T4 with the free ends of its long tail fibers (1, 26, 51). These fibers consist of four proteins: p34, p35, p36, and p37. p37 constitutes the distal part of the fiber and mediates receptor recognition (2, 51) with an area near its C terminus (17, 32). p34, p36, and p37 in these tail fibers are oligomers. It had earlier been assumed that they form dimers (50, 53); most likely, however, they are trimers. There is experimental evidence for the trimeric state of p34 and p37 (8), and regarding p37, strong indirect evidence stems from the fact that the tail fibers of phage T7 consist of trimers of this virion's p17 (49). Tail fiber genes are of a mosaic structure (summarized in reference 16), very strongly indicating horizontal transfer of gene fragments. Corresponding protein fragments, partially identical to sequences of p17, exist in p37 of phages K3 and T2 (16), which are very closely related to T4. There is little doubt, therefore that all p37 proteins are trimeric. Assembly of these fibers requires helpers (for a recent review, see reference 54), which are absent from the mature virion. In the absence of one of these, p38, p37 fails to oligomerize. A gene 38 (g38) partial bypass mutant has been isolated (3), and it has been shown to consist of a duplication of residues 797 to 805 (17) of the 1,026-residue p37 (36). This is the area where p38 is believed to act on p37 (48). Infection with the mutant phage leads to about 30% assembled distal half-fibers (compared with the amount produced in wild-type phage infectio...

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Structure of bacteriophage T4 genes 37 and 38

Cited by 54 publications

References 20 publications

Characterization of two polyvalent phages infecting Enterobacteriaceae

Characterization of two polyvalent phages infecting Enterobacteriaceae

DNA sequences of the tail fiber genes of bacteriophage P2: evidence for horizontal transfer of tail fiber genes among unrelated bacteriophages

Characterization of the helper proteins for the assembly of tail fibers of coliphages T4 and lambda

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