The uncoating of alfalfa mosaic virus by its own RNA

Vloten-Doting, Lous Van; Jaspars, E.M.J.

doi:10.1016/0042-6822(72)90154-7

Cited by 147 publications

(42 citation statements)

References 13 publications

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“…The evidence for the importance of RNA-CP interactions in the life cycle of AlMV has lead to several studies on the identification of CP binding determinants in the AlMV RNAs. The observation that AlMV RNAs are able to withdraw CP subunits from virus particles in vitro indicated that the RNAs contain specific binding sites with a high affinity for CP (10). In subgenomic RNA 4, which is identical in sequence to the 3′-terminal sequence of 881 nucleotides (nt) of RNA 3, these high-affinity binding sites were predominantly localized in the 3′-terminal untranslated region (UTR) (11).…”

Section: Introductionmentioning

confidence: 99%

“…The importance of the AUGC-motifs for CP binding was further illustrated by Houser-Scott et al (13) who demonstrated that mutation of the second AUGC-motif in the 3′-terminal 39 nt fragment of RNA 3 resulted in a loss of CP binding. Moreover, these authors showed that poly(AUGC) 10 was unable to bind CP, indicating that the AlMV CP recognizes invariant AUGC motifs in the context of conserved structural elements. In this study we investigated determinants for CP binding in the extreme 3′-terminal 39 nt of RNA 3.…”

Section: Introductionmentioning

confidence: 99%

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Structural Elements of the 3'-Terminal Coat Protein binding Site in Alfalfa Mosaic Virus RNAs

Reusken

Bol

1996

Nucleic Acids Research

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The 3′-termini of the three genomic RNAs of alfalfa mosaic virus (AlMV) and ilarviruses contain a number of AUGC-motifs separated by hairpin structures. Binding of coat protein (CP) to such elements in the RNAs is required to initiate infection of these viruses. Determinants for CP binding in the 3′-terminal 39 nucleotides (nt) of AlMV RNA 3 were analyzed by band-shift assays. From the 5′-to 3′-end this 39 nt sequence contains AUGC-motif 3, stem-loop structure 2 (STLP2), AUGC-motif 2, stem-loop structure 1 (STLP1) and AUGC-motif 1. A mutational analysis showed that all three AUGC-motifs were involved in CP binding. Mutation of the A-and U-residues of motifs 1 or 3 had no effect on CP binding but similar mutations in motif 2 abolished CP binding. A mutational analysis of the stem of STLP1 and STLP2 confirmed the importance of these hairpins for CP binding. Randomization of the sequence of the stems and loops of STLP1 and STLP2 had no effect on CP binding as long as the secondary structure was maintained. This indicates that the two hairpins are not involved in sequence-specific interactions with CP. They may function in a secondary structure-specific interaction with CP and/or in the assembly of the AUGC-motifs in a configuration required for CP binding.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Structural Elements of the 3'-Terminal Coat Protein binding Site in Alfalfa Mosaic Virus RNAs

Reusken

Bol

1996

Nucleic Acids Research

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“…AMV, which was the kind gift of Mr A. Bialer, was propagated in tobacco and isolated according to the method of van Vloten-Doting & Jaspers (1972). Wheat germ S-30 was prepared as described by Roberts & Paterson (1973).…”

Section: Discussionmentioning

confidence: 99%

Translational Competition Between Related Virus RNA Species in Cell-free Systems

Salomon

Bar‐Joseph

1982

Journal of General Virology

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“…Inoculated leaves from infected plants were collected 1-10 days after inoculation. Virus particles were isolated from these leaves as described by van Vloten-Doting and Jaspars (17). RNA extracted from protoplast samples and purified virus particles was analysed, after glyoxylation and electrophoresis in 1% agarose gels by Northern blot hybridization using random primed cDNA3 as probe (18 …”

Section: Rna Analysismentioning

confidence: 99%

Role of the 5′ leader sequence of alfalfa mosaic virus RNA 3 in replication and translation of the viral RNA

1993

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RNA 3 of alfalfa mosaic virus (AIMV) encodes the movement protein P3 and the viral coat protein which is translated from the subgenomic RNA 4. The 5'-leader sequences of RNA 3 of AIMV strains S, A, and Y differ in length from 314 to 392 nucleotides and contain a variable number of internal control regions of type 2 (ICR2 motifs) each located in a 27 nt repeat. Infectious cDNA clones were used to exchange the leader sequences of the three strains. This revealed that the leader sequence controls the specific ratio in which RNAs 3 and 4 are synthesized for each strain. In addition, it specifies strain specific differences in the kinetics of P3 accumulation in plants. Subsequent deletion analysis revealed that a 5'-sequence of 1 12 nt containing one ICR2 motif was sufficient for a 10 to 20% level of RNA 3 accumulation in protoplasts and a delayed accumulation in plants. An

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The uncoating of alfalfa mosaic virus by its own RNA

Cited by 147 publications

References 13 publications

Structural Elements of the 3'-Terminal Coat Protein binding Site in Alfalfa Mosaic Virus RNAs

Structural Elements of the 3'-Terminal Coat Protein binding Site in Alfalfa Mosaic Virus RNAs

Translational Competition Between Related Virus RNA Species in Cell-free Systems

Role of the 5′ leader sequence of alfalfa mosaic virus RNA 3 in replication and translation of the viral RNA

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