Baseplate hub assembly chaperone gp51 of bacteriophage T4 required during the late phase of infection for the formation of the central hub of the tail baseplate. Synthesized in very low copy numbers in the infected host cell and absent from mature virions, gp51 acts transiently alongside group II hub components (gp5, gp26, gp27, gp28, and gp29) to promote assembly of a functional central baseplate plug onto which the six peripheral baseplate wedges circularize.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0098003 viral tail assembly | IEA GO_REF:0000043 | ACCEPT | Reason: gp51 is an essential group II baseplate hub assembly chaperone required for formation of the central hub of the bacteriophage T4 tail baseplate during late viral morphogenesis. Supporting Evidence: file:BPT4/51/51-uniprot.txt FUNCTION: Chaperone that is involved in the formation of the central hub of the baseplate. {ECO:0000303|PubMed:21129200}. file:BPT4/51/51-deep-research-falcon.md Across authoritative sources, gp51 is consistently described as being required for formation of the baseplate hub (matsui1997isolationandcharacterization pages 1-2) and annotated explicitly as a βhub assembly chaperoneβ |
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Download this section (compressed HTML)Q: Which specific central hub protein (gp5, gp26, gp27, gp28, or gp29) is the direct substrate of gp51 during baseplate hub assembly?
Q: Does gp51 act solely as a conformational holdase/assembly factor, or does it catalyze a covalent or proteolytic maturation event (such as N-terminal processing of gp26) during hub assembly?
Experiment: Perform yeast two-hybrid and in vitro co-immunoprecipitation screens testing purified recombinant gp51 against individual and co-expressed hub components (gp5, gp26, gp27, gp28, gp29) to identify its direct binding partner(s).
Experiment: Disrupt the translational-repressing RNA stem-loop at the gene 51 ribosome-binding site to overproduce gp51 during T4 infection and test whether excess gp51 sequesters hub subunits or alters baseplate assembly efficiency.
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