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Gene Review

6K2  - 

Sweet potato feathery mottle virus

 
 
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Disease relevance of 6K2

  • Mutations at the 6K2/VPg cleavage site reduced virus infectivity in plants, but had a less pronounced, albeit detectable, effect on proteolytic processing in the baculovirus system [1].
  • Deletion of various portions, or insertion of six histidine residues (6xHis) into various positions of the membrane-bound 6K2 protein (53 amino acids) of Potato virus A (PVA, genus Potyvirus), inhibited systemic infection in Nicotiana tabacum and N. benthamiana plants [2].
  • Amino acid sequence comparison with poty- and rymoviruses reveals eight domains corresponding to the potyviral P3, 6K1, Cl, 6K2, Nla-VPg, Nla-Pro, Nlb and capsid proteins, respectively [3].
 

High impact information on 6K2

  • However, deletion of either the 6K1 or 6K2 protein-encoding regions rendered PVA non-infectious [1].
  • Amino acid substitutions at three additional positions of the central part (aa 116) and C terminus (aa 185) of the VPg and of the N terminus of the 6K2 protein (aa 5) affect virus accumulation and rate of systemic infection but are not sufficient for phloem loading of PVA [4].
  • Both 6K peptides are indispensable for virus replication, and proteolytic separation of the 6K2 protein from the adjacent proteins by NIaPro is important for the rate of virus replication and movement [1].
 

Biological context of 6K2

  • Although sequence identities over most of the genome were well above 90% at both the nt and aa levels, reaching 99.6% (aa) in the CP and 100% (aa) in the 6K1 and 6K2, thereby suggesting that WMV-Pk and WMV-Fr are identical strains, but the sequence identities in the P1 region were only 80.6% (aa) and 82.8% (nt), while that in the 5' UTR was 82% [5].
 

Other interactions of 6K2

  • In particular, the most considerable divergence has been found in part of 5' non coding region, in regions encoding P1, P3 + 6K1, 6K2 and NIa-VPg proteins as well as in the N-terminal domain of the coat protein [6].
 

Analytical, diagnostic and therapeutic context of 6K2

References

  1. Proteolytic processing of potyviral proteins and polyprotein processing intermediates in insect and plant cells. Merits, A., Rajamäki, M.L., Lindholm, P., Runeberg-Roos, P., Kekarainen, T., Puustinen, P., Mäkeläinen, K., Valkonen, J.P., Saarma, M. J. Gen. Virol. (2002) [Pubmed]
  2. Potyviral 6K2 protein long-distance movement and symptom-induction functions are independent and host-specific. Spetz, C., Valkonen, J.P. Mol. Plant Microbe Interact. (2004) [Pubmed]
  3. The complete nucleotide sequence of barley mild mosaic virus RNA1 and its relationship with other members of the Potyviridae. Meyer, M., Dessens, J.T. Virology (1996) [Pubmed]
  4. Viral genome-linked protein (VPg) controls accumulation and phloem-loading of a potyvirus in inoculated potato leaves. Rajamäki, M.L., Valkonen, J.P. Mol. Plant Microbe Interact. (2002) [Pubmed]
  5. The complete nucleotide sequence of a Pakistani isolate of Watermelon mosaic virus provides further insights into the taxonomic status in the Bean common mosaic virus subgroup. Ali, A., Natsuaki, T., Okuda, S. Virus Genes (2006) [Pubmed]
  6. The complete nucleotide sequence of Plum pox virus isolates from sweet (PPV-SwC) and sour (PPV-SoC) cherry and their taxonomic relationships within the species. Fanigliulo, A., Comes, S., Maiss, E., Piazzolla, P., Crescenzi, A. Arch. Virol. (2003) [Pubmed]
  7. The 6K2 protein and the VPg of potato virus A are determinants of systemic infection in Nicandra physaloides. Rajamäki, M.L., Valkonen, J.P. Mol. Plant Microbe Interact. (1999) [Pubmed]
 
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