“…In contrast, the RNA 3′‐portion undergoes an about five to three times slower, noncooperative encapsidation by small CP oligomers such as A‐protein and monomers (Butler & Lomonossoff, ; Fukuda, Ohno, Okada, Otsuki, & Takebe, ; Otsuki, Takebe, Ohno, Fukuda, & Okada, ; Turner, McGuigan, & Butler, ). Although there is some bias towards G residues in the third positions along the wildtype TMV RNA, thought to stabilize the assembled complex (Steckert & Schuster, ; Wilson & McNicol, ), numerous heterologous OAs‐containing RNA sequences have been packaged efficiently with TMV CP in vitro, and endogenous plant transcripts can be found in natural virus particles (the original references are briefly reviewed in Schneider et al, ). Hence, except for the OAs nucleotide stretch folding into its major stem‐loop A (position 5,447–5,515 of the TMV vulgare sequence, National Center for Biotechnology Information NCBI reference NC_001367.1 (Butler, ; Goelet et al, ; Zimmern, ), no further sequence prerequisites seem essential for the scaffolding function of the integral TMV RNA (see also Altintoprak et al, ).…”