On 2015 Jan 28, Donald Forsdyke commented:

SIMILARITY BETWEEN EPSTEIN-BARR VIRUS AND PLASMODIUM FALCIPARUM. A key observation in this paper (Cristillo et al. 2001) is that the EBNA-1 protein is longer than necessary because of the need to contain a low complexity GLY-ALA repeat region between functional domains. This allows purine-loading at the nucleic acid level. Essentially the same observation was reported by Pizzi and Frontali (Genome Research 2001 11, 218-229). They noted:

"Proteins from Plasmodium falciparum, the etiological agent of the most severe form of human malaria, are often larger than homologous proteins from other organisms. When multiple alignment is possible, the size difference can be seen to be due to the presence of long insertions separating well-conserved blocks that are adjacent in the homologous proteins.... The insertions are characterized by highly recurrent amino acid usage" and correspond to "low complexity regions ... believed to encode non-globular domains of unknown function that are extruded from the protein core and do not impair the functional folding of the protein."... The recurrent amino acids "correlate with A-richness in codons."

This quotation from Pizzi and Frontali is the first of a series of End Notes that were added to the version of the Cristillo paper displayed on one of Forsdyke's webpages http://post.queensu.ca/~forsdyke/EBV.htm

On 2015 Jan 28, Donald Forsdyke commented:

SIMILARITY BETWEEN EPSTEIN-BARR VIRUS AND PLASMODIUM FALCIPARUM. A key observation in this paper (Cristillo et al. 2001) is that the EBNA-1 protein is longer than necessary because of the need to contain a low complexity GLY-ALA repeat region between functional domains. This allows purine-loading at the nucleic acid level. Essentially the same observation was reported by Pizzi and Frontali (Genome Research 2001 11, 218-229). They noted:

"Proteins from Plasmodium falciparum, the etiological agent of the most severe form of human malaria, are often larger than homologous proteins from other organisms. When multiple alignment is possible, the size difference can be seen to be due to the presence of long insertions separating well-conserved blocks that are adjacent in the homologous proteins.... The insertions are characterized by highly recurrent amino acid usage" and correspond to "low complexity regions ... believed to encode non-globular domains of unknown function that are extruded from the protein core and do not impair the functional folding of the protein."... The recurrent amino acids "correlate with A-richness in codons."

This quotation from Pizzi and Frontali is the first of a series of End Notes that were added to the version of the Cristillo paper displayed on one of Forsdyke's webpages http://post.queensu.ca/~forsdyke/EBV.htm