ArticleMolecular microbiology2008
Origin and function of the two major tail proteins of bacteriophage SPP1.
Article in Molecular microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 48 citations in OpenAlex.
- Dual function of a highly conserved bacteriophage tail completion protein essential for bacteriophage infectivity.Communications biology · 2024Article
- Real-time detection of virus antibody interaction by label-free common-path interferometry.Biophysical reports · 2023Article
- Morphological and Genetic Characterization ofViruses · 2022Article
- Tall tails: cryo-electron microscopy of phage tail DNA ejection conduits.Biochemical Society transactions · 2022Article
- Temporal compartmentalization of viral infection in bacterial cells.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Bi- and Multi-directional Gene Transfer in the Natural Populations of Polyvalent Bacteriophages, and Their Host Species Spectrum Representing Foodborne Versus Other Human and/or Animal Pathogens.Food and environmental virology · 2021Article
- Architecture of the flexible tail tube of bacteriophage SPP1.Nature communications · 2020Article
- Galaxy and Apollo as a biologist-friendly interface for high-quality cooperative phage genome annotation.PLoS computational biology · 2020Article
- Regulators of Viral Frameshifting: More Than RNA Influences Translation Events.Annual review of virology · 2020Review
- Conserved and Diverse Traits of Adhesion Devices fromViruses · 2020Review
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- Bacteriophage T5 tail tube structure suggests a trigger mechanism for Siphoviridae DNA ejection.Nature communications · 2017Article
- Comparative genomics and functional analysis of the 936 group of lactococcal Siphoviridae phages.Scientific reports · 2016Article
- Structural proteins ofBacteriophage · 2016Article
- Structural rearrangements in the phage head-to-tail interface during assembly and infection.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Virus evolution toward limited dependence on nonessential functions of the host: the case of bacteriophage SPP1.Journal of virology · 2015Article
- Bacteriophage SPP1 tail tube protein self-assembles into β-structure-rich tubes.The Journal of biological chemistry · 2015Article
- The collagen-like protein gp12 is a temperature-dependent reversible binder of SPP1 viral capsids.The Journal of biological chemistry · 2014Article
- Insights into bacteriophage T5 structure from analysis of its morphogenesis genes and protein components.Journal of virology · 2014Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The majority of bacteriophages have a long non-contractile tail (Siphoviridae) that serves as a conduit for viral DNA traffic from the phage capsid to the host cell at the beginning of infection. The 160-nm-long tail tube of Bacillus subtilis bacteriophage SPP1 is shown to be composed of two major tail proteins (MTPs), gp17.1 and gp17.1*, at a ratio of about 3:1. They share a common amino-terminus, but the latter species has approximately 10 kDa more than gp17.1. A CCC.UAA sequence with overlapping proline codons at the 3' end of gene 17.1 drives a programmed translational frameshift to another open reading frame. The recoding event generates gp17.1*. Phages carrying exclusively gp17.1 or gp17.1* are viable, but tails are structurally distinct. gp17.1 and the carboxyl-terminus of gp17.1* have a distinct evolutionary history correlating with different functions: the polypeptide sequence identical in the two proteins is responsible for assembly of the tail tube while the additional module of gp17.1* shields the structure exterior exposed to the environment. The carboxyl-terminal extension is an elaboration present in some tailed bacteriophages. Different extensions were found to combine in a mosaic fashion with the MTP essential module in a subset of Siphoviridae genomes.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.