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PMID:24889236
| Citation |
Oh, B, Moyer, CL, Hendrix, RW and Duda, RL (2014) The delta domain of the HK97 major capsid protein is essential for assembly. Virology 456-457:171-8 |
|---|---|
| Abstract |
The 102 residue N-terminal extension of the HK97 major capsid protein, the delta domain, is normally present during the assembly of immature HK97 procapsids, but it is removed during maturation like well-known internal scaffolding proteins of other tailed phages and herpesviruses. The delta domain also shares other unusual properties usually found in other viral and phage scaffolding proteins, including its location on the inside of the capsid, a high predicted and measured α-helical content, and an additional prediction for the ability to form parallel coiled-coils. Viral scaffolding proteins are essential for capsid assembly and phage viability, so we tested whether the HK97 delta domain was essential for capsid assembly. We studied the effects of deleting all or parts of the delta domain on capsid assembly and on complementation of capsid-protein-defective phage, and our results demonstrate that the delta domain is required for HK97 capsid assembly. |
| Links |
PubMed PMC4044616 Online version:10.1016/j.virol.2014.03.022 |
| Keywords |
Bacteriophages/genetics; Bacteriophages/physiology; Capsid Proteins/genetics; Capsid Proteins/metabolism; DNA Mutational Analysis; Protein Structure, Tertiary; Sequence Deletion; Virus Assembly |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0046797: viral procapsid maturation |
ECO:0000315: |
P |
HK97 delta domain is necessary for proper procapsid assembly. HK97 delta domain comprises the first 102 amino acids of the major capsid protein, is present during procapsid assembly, and is cleaved during capsid maturation. In Figure 2A, HK97 lacking the delta domain was found to have become insoluble. Figure 2B shows similar results, with delta-less HK97 present only in the pellet fraction (as marked by a circle). Figure 2C shows expression of a full-length HK97 protein plasmid (protease-) and delta-less HK97. Full-length HK97 is shown to properly form capsomers and proheads—signs of proper assembly— while the lack of bands for the delta-less HK97 show there is no formation of capsomers or proheads. From this, we can conclude that the delta-domain of HK97 is necessary for formation of a properly folded, soluble procapsid head. |
complete | ||||
Notes
See also
References
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