Interaction of the Cauliflower Mosaic Virus Coat Protein with the Pregenomic RNA Leader

Guerra‐Peraza, Orlene; Tapia, Marc de; Höhn, Thomas; Hemmings‐Mieszczak, Maja

doi:10.1128/jvi.74.5.2067-2072.2000

Cited by 40 publications

(35 citation statements)

References 48 publications

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“…It is unlikely that CaMV CP and the viral DNA cosediment in the same fraction without interacting, because CaMV pregenomic RNA has been shown to interact with viral CP in vitro (11), and CaMV DNA replication depends on the presence of the CP precursor (K.K. and T.H., submitted).…”

Section: Resultsmentioning

confidence: 99%

The Cauliflower Mosaic Virus Virion-Associated Protein Is Dispensable for Viral Replication in Single Cells

Kobayashi

Tsuge

Stavolone

et al. 2002

J Virol

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Section: Resultsmentioning

confidence: 99%

The Cauliflower Mosaic Virus Virion-Associated Protein Is Dispensable for Viral Replication in Single Cells

Kobayashi

Tsuge

Stavolone

et al. 2002

J Virol

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“…It remains an open question whether CP44 or CP37 is the mature virus capsid protein. Here we provided evidence that the processing of CP44 into CP37 implies the removal of the phosphorylation sites and of the Zn finger motif, both of which are essential for infectivity (7,16). We assume that the removed polypeptides are required early in infection, e.g., in the assembly and/or reverse transcription process.…”

Section: Figmentioning

confidence: 99%

“…Such regulation may occur intra-or intermolecularly. This hypothesis is attractive since the strong nucleic acid binding activity of CP56 (1,9) needs to be tightly regulated to allow the specific packaging of the RNA pregenome, notwithstanding the timing between packaging and reverse transcription (7).…”

Section: Figmentioning

confidence: 99%

“…The acidic domain is followed by a short nuclear localization signal (13), an assembly domain (1), and a large cluster of basic amino acids involved in nucleic acid binding (1,4), including a Zn finger motif specifying interaction with a packaging signal located on the CaMV RNA leader sequence (7). CP44 starts with amino acid 77 of the precursor protein (16); however, neither the N termini of CP39 and CP37 nor the C termini of any of these proteins are precisely known.…”

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confidence: 99%

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Mutation of Capsid Protein Phosphorylation Sites Abolishes Cauliflower Mosaic Virus Infectivity

Chapdelaine

Kirk

Karsies

et al. 2002

J Virol

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The cauliflower mosaic virus (CaMV) capsid protein is derived by bidirectional processing of the precapsid protein (CP56). We expressed several derivatives of CP56 in Escherichia coli and used them as substrates for virus-associated kinase and casein kinase II purified from plant cells. Three serine residues located at the N terminus of the mature viral protein CP44 were identified as phosphorylation targets. A mutation of one of them in the viral context had little or no effect on viral infectivity, but a mutation of all three serines abolished infectivity. The mapping of phosphorylation sites in CP44, but not CP39 or CP37, and immunodetection of the Zn finger motif in CP44 and CP39, but not CP37, support the model that CP39 is produced from CP44 by N-terminal processing and CP37 is produced from CP39 by C-terminal processing. We discuss the possible role of phosphorylation in the processing and assembly of CaMV capsid protein.The structural proteins of retroviruses and pararetroviruses are modified by proteolysis, phosphorylation (5, 6), ubiquitination (23, 18), glycosylation (3, 19), meristylation, and other reactions. In many cases, these modifications have been shown to control assembly, genome packaging and release, and intracellular transport and distribution (2). The best studied of the plant pararetroviruses is cauliflower mosaic virus (CaMV). Its precapsid protein (CP56) is 489 amino acids long (Fig. 1A). Several processing steps lead to three main capsid protein species, CP44, CP39, and CP37 (named after their respective mobilities, in kilodaltons, on sodium dodecyl sulfate [SDS]-polyacrylamide gel electrophoresis [PAGE]), that share the same central sequence but differ in their termini (1,4,16). This is in contrast to the structural proteins of retroviruses, which represent different, nonoverlapping domains (MA, CA, and NC) of the precursor Gag protein, or to the hepatitis B virus (HBV) C protein, which is not cleaved.CP44, but not CP39 or CP37, contains an acidic N-terminal sequence, which also includes serine, threonine, and proline residues, a combination that frequently renders proteins unstable (12). The acidic domain is followed by a short nuclear localization signal (13), an assembly domain (1), and a large cluster of basic amino acids involved in nucleic acid binding (1, 4), including a Zn finger motif specifying interaction with a packaging signal located on the CaMV RNA leader sequence (7). CP44 starts with amino acid 77 of the precursor protein (16); however, neither the N termini of CP39 and CP37 nor the C termini of any of these proteins are precisely known. Additional domains characterized by acidic residues, serine, and threonine and leading to protein instability make up the N and C termini of CP56 (12).A virion-associated enzyme (17) with casein kinase II (CK II) properties (16) phosphorylates CP44, but not CP39 or CP37. In the experiments leading to these results, substrates and enzymatic activity in the same preparation were evaluated. In the present study, CaMV CP derivatives were...

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“…The alternative shunt becomes apparent when the primary shunt has been impaired. The function of the second shunt might be just to contribute to a tighter protection of the central leader structure, which is thought to be required for packaging (36).…”

Section: Discussionmentioning

confidence: 99%

Continuous and Discontinuous Ribosome Scanning on the Cauliflower Mosaic Virus 35 S RNA Leader Is Controlled by Short Open Reading Frames

Ryabova

Pooggin²,

Dominguez³

et al. 2000

Journal of Biological Chemistry

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The pathways of scanning ribosome migration controlled by the cauliflower mosaic virus 35 S RNA leader were investigated in vitro and in vivo. This long (600 nucleotides) leader contains several short open reading frames (sORFs) and folds into an extended hairpin structure with three main stable stem sections. Translation initiation downstream of the leader is cap-dependent and occurs via ribosomal shunt under the control of two cis elements, a short open reading frame A (sORF A) followed by stem section 1. Here we show that a second similar configuration comprising sORF B followed by stem section 2 also allows shunting. The efficiency of the secondary shunt was greatly increased when stem section 1 was destabilized. In addition, we present evidence that a significant fraction of reinitiation-competent ribosomes that escape both shunt events migrate linearly via the structured central region but are intercepted by internal AUG start codons. Thus, expression downstream of the 35 S RNA leader is largely controlled by its multiple sORFs.

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Interaction of the Cauliflower Mosaic Virus Coat Protein with the Pregenomic RNA Leader

Cited by 40 publications

References 48 publications

The Cauliflower Mosaic Virus Virion-Associated Protein Is Dispensable for Viral Replication in Single Cells

The Cauliflower Mosaic Virus Virion-Associated Protein Is Dispensable for Viral Replication in Single Cells

Mutation of Capsid Protein Phosphorylation Sites Abolishes Cauliflower Mosaic Virus Infectivity

Continuous and Discontinuous Ribosome Scanning on the Cauliflower Mosaic Virus 35 S RNA Leader Is Controlled by Short Open Reading Frames

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