Assembly of bacteriophage T4 tail fibers: Identification and characterization of the nonstructural protein gp57

Herrmann, Richard; Wood, William B.

doi:10.1007/bf00271208

Cited by 15 publications

(9 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Their coding sequences start at position 105 and 123, respectively, but both terminate at position 285 using the same reading frame. Their molecular weights agree well with the molecular weight of the single polypeptide (about 6000 daltons), that is synthesized in vivo in E. coli under direction of the cloned T4 DNA fragment (3). The direction of protein synthesis for the supposed gp57A is in accordance with the direction of transcription of that region in T4 infected E. coli (13).…”

Section: Discussionsupporting

confidence: 66%

“…Final proof for the identity of gp57A can only be derived from amino acid analysis of the N-terminus of that protein. Cloning experiments have shown that gene 57 is expressed independently of its orientation in the phage fd vector (3). This suggests that the signal sequences for transcription (16) and translation (17,18) are contained in the cloned T4 DNA fragment.…”

Section: Discussionmentioning

confidence: 99%

“…Amber mutations in gene 57 can be complemented by a cloned, about 700 bp long,fragment of phage T4 DNA. This cloned DNA fragment directs in E. coli the synthesis of a single poly-peDtide, that appears to be identical with gp57A, indicating that this polypeptide is the only essential gene product missing in gene 57 amber mutants and that gp57B is not essential for morphogenesis of these mutants (3). Functionally, gp57A belongs to a class of nonstructural, accessory proteins, that mediate assembly of structural proteins into a more complex organisation (1).…”

Section: Introductionmentioning

confidence: 99%

“…The nucleotide sequence should not only provide the primary structure of gp57A, it should also help to explain genetic data, e.g. the finding that all gene 57 amber mutants appear to represent mutations at a single site (2) and the observation that two phage proteins are lost as a result of single amber mutations in gene 57 (3).…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Nucleotide sequence of the bacteriophage T4 gene 57 and a deduced amino acid sequence

Herrmann

1982

Nucl Acids Res

Self Cite

View full text Add to dashboard Cite

A 693 basepair cloned fragment of bacteriophage T4 DNA, which supports specifically growth of T4 amber mutants in gene 57, has been sequenced. A polypeptide can be deduced from this sequence, that is either 54 or 60 amino acids long depending which of two AUG codons, 18 nucleotides apart, are used for initiation. The size of this deduced polypeptide is compatible with the size of a single polypeptide (based on polyacrylamide gel electrophoresis) synthesized in vivo in E. coli under the direction of the cloned T4 DNA fragment.

show abstract

Section: Discussionsupporting

confidence: 66%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Nucleotide sequence of the bacteriophage T4 gene 57 and a deduced amino acid sequence

Herrmann

1982

Nucl Acids Res

Self Cite

View full text Add to dashboard Cite

show abstract

“…Chaperone P57A participates in the assembly of P34 and P37 and also in the assembly of the short TF, P12 (15,19). P38 is necessary (in addition to P57A) for the trimerization of gp37 to form the mature P37 rod, which initiates the extension of LTF assembly (9, 13).…”

mentioning

confidence: 99%

In Vivo Bypass of Chaperone by Extended Coiled-Coil Motif in T4 Tail Fiber

Hyman

Harrah

et al. 2004

J Bacteriol

View full text Add to dashboard Cite

The distal-half tail fiber of bacteriophage T4 is made of three gene products: trimeric gp36 and gp37 and monomeric gp35. Chaperone P38 is normally required for folding gp37 peptides into a P37 trimer; however, a temperature-sensitive mutation in T4 (ts3813) that suppresses this requirement at 30°C but not at 42°C was found in gene 37 (R. J. Bishop and W. B. Wood, Virology 72:244-254, 1976). Sequencing of the temperaturesensitive mutant revealed a 21-bp duplication of wild-type gene 37 inserted into its C-terminal portion (S. Hashemolhosseini et al., J. Mol. Biol. 241:524-533, 1994). We noticed that the 21-amino-acid segment encompassing this duplication in the ts3813 mutant has a sequence typical of a coiled coil and hypothesized that its extension would relieve the temperature sensitivity of the ts3813 mutation. To test our hypothesis, we crossed the T4 ts3813 mutant with a plasmid encoding an engineered pentaheptad coiled coil. Each of the six mutants that we examined retained two amber mutations in gene 38 and had a different coiled-coil sequence varying from three to five heptads. While the sequences varied, all maintained the heptad-repeating coiled-coil motif and produced plaques at up to 50°C. This finding strongly suggests that the coiled-coil motif is a critical factor in the folding of gp37. The presence of a terminal coiled-coil-like sequence in the tail fiber genes of 17 additional T-even phages implies the conservation of this mechanism. The increased melting temperature should be useful for "clamps" to initiate the folding of trimeric ␤-helices in vitro and as an in vivo screen to identify, sequence, and characterize trimeric coiled coils.Escherichia coli bacteriophage T4 is a complex nanomachine assembled from DNA and protein. It is composed of four major structural components: a genome of DNA, a head, a tail, and tail fibers (TFs) (Fig. 1). Most, or all, T4 virion structural proteins are transcribed and translated during the late period of infection. The assembly processes of the three protein structural components (head, tail, and TFs) occur in parallel with the aid of a group of chaperones (39,40). Nearly all of these chaperones are proteins encoded by genes in the T4 genome (10). They help to regulate the folding and assembly of T4 proteins and are not included in the final functional structure of the virion.The T4 long TFs (LTFs) are critical for the first steps of viral infection (11,12). The chemosensors in the carboxy-terminal region of the LTFs recognize the host cell by binding (reversibly) to receptors displayed on the cell surface (14). The phage then attaches to the cell irreversibly via P12 (short TFs) (31). Each LTF on the phage has a rod-like structure that consists of proximal-and distal-half TFs of approximately equal lengths, joined at their ends in an angle (39). Proximal-half LTFs are parallel homotrimers of matured gp34 (called P34, where P denotes the homooligomeric assembly of the monomeric gene product, gp34). Distal-half fibers contain a monomer of gp35, a homotrimer of ...

show abstract

Transformation of tobacco protoplasts with DNA entrapped in pH-sensitive liposomes

Zhu¹,

Hughes

Huang

1990

Plant Cell Tiss Organ Cult

View full text Add to dashboard Cite

A system for the transformation of tobacco mesophyll protoplasts using pH-sensitive liposomes was developed. Plasmid DNA (plGVneo23) encoding the NPT-II gene for kanamycin resistance was entrapped in pH-sensitive liposomes composed of dioleolphosphatidylethanolamine, cholesterol and oleic acid. These liposomes release their contents at low pH and are capable of delivering their contents into the cytoplasm of protoplasts. Kanamycin-resistant colonies were reproducibly recovered from transformed protoplasts at an average frequency of 1.62 x 10 -4 at pH 7.5. Plants regenerated from transformed cell lines were normal in appearance and were fertile. NPT-II activity was detected in leaf extracts of transformed, kanamycin-resistant plants and the presence of NPT-II DNA in the tobacco genome was shown by Southern blots. Analysis of self-pollinations and reciprocal crosses to non-transformed plants indicated that kanamycin resistance segregated as a dominant nuclear marker. Co-transformation of protoplasts with liposomes containing two selectable markers indicated that co-transformation occurred with a frequency of approximately 23%.

show abstract

Assembly of bacteriophage T4 tail fibers: Identification and characterization of the nonstructural protein gp57

Cited by 15 publications

References 31 publications

Nucleotide sequence of the bacteriophage T4 gene 57 and a deduced amino acid sequence

Nucleotide sequence of the bacteriophage T4 gene 57 and a deduced amino acid sequence

In Vivo Bypass of Chaperone by Extended Coiled-Coil Motif in T4 Tail Fiber

Transformation of tobacco protoplasts with DNA entrapped in pH-sensitive liposomes

Contact Info

Product

Resources

About