Analysis of the protein composition of alfalfa mosaic virus RNA-dependent RNA polymerase

Quadt, R.; Rosdorff, H.J.M.; Hunt, Tim; Jaspars, E.M.J.

doi:10.1016/0042-6822(91)90674-z

Cited by 77 publications

(51 citation statements)

References 19 publications

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“…The genome of brome mosaic virus (BMV; bromovirus group; 'Sindbis-like' supergroup of plant viruses) encodes a helicase-like protein, named the la protein (Hodgman, 1988), which is required for continued accumulation of all classes of BMV RNA (positive-strand, negative-strand and subgenomic) (Kroner et al, 1990). In agreement with the presumed necessity of an unwinding activity for RNA replication, it has been found that an RNA helicase activity is present in RNA polymerase preparations of encephalomyocarditis virus (a picornavirus; Dmitrieva et al, 1991) and alfalfa mosaic virus (ilarvirus group; Quadt et al, 1991). Moreover, an in vitro replication system able to catalyse complete replication of cucumber mosaic virus (CMV) RNAs has been developed recently (Hayes & Buck, 1990), and it was shown that the helicase-like CMV protein is an essential subunit of the purified RNA-dependent RNA polymerase (Hayes & Buck, 1990).…”

Section: Genome Replicationmentioning

confidence: 89%

Highlights and prospects of potyvirus molecular biology

Riechmann

Laı́n

Garcı́a

1992

Journal of General Virology

567

355

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Section: Genome Replicationmentioning

confidence: 89%

Highlights and prospects of potyvirus molecular biology

Riechmann

Laı́n

Garcı́a

1992

Journal of General Virology

567

355

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“…In addition to genome activation, interactions between AlMV CP and RNAs have been implicated in RNA stability (3), RNA replication (4,5), a switch from minus-strand RNA synthesis to plus-strand RNA synthesis (6)(7)(8) and cell-to-cell spread (9). 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.…”

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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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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“…Evidence was obtained that CP has a trans-acting function in regulation of the balance of viral plus-and minus-strand RNA synthesis (8). A role of CP in RNA replication was further supported by the finding that, in addition to PI and P2, CP is present in the purified AIMV replicase complex (9). Such a role is probably specific for AIMV and ilarviruses as no CP was found in the purified replicase of the cucumovirus cucumber mosaic virus (CMV; 10).…”

Section: Introductionmentioning

confidence: 51%

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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Analysis of the protein composition of alfalfa mosaic virus RNA-dependent RNA polymerase

Cited by 77 publications

References 19 publications

Highlights and prospects of potyvirus molecular biology

Highlights and prospects of potyvirus molecular biology

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

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

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