The complete nucleotide sequence of apple mosaic virus (ApMV) RNA 1 and RNA 2: ApMV is more closely related to alfalfa mosaic virus than to other ilarviruses

The complete nucleotide sequences of apple mosaic virus RNA 1 and 2 have been characterized. Apple mosaic virus RNA 1 is 3476 nucleotides in length and encodes a single large open reading frame (ORF), whereas apple mosaic virus RNA 2 is 2979 nucleotides in length and also encodes a single ORF. The amino acid sequences encoded by RNA 1 and 2 show similarity to all of the other ilarviruses for which sequence data are available, but both are more closely related to alfalfa mosaic virus (AMV) than to other ilarviruses. Points of similarity include the absence of ORF 2b, present on the RNA 2 of all previously characterized ilarviruses. The close relationship to AMV also occurs in the movement protein, encoded by RNA 3, but not with the coat protein. These data suggest that the present taxonomy should be revised, and that AMV should be considered an aphid-transmissible ilarvirus.

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Role of a Short Open Reading Frame in Ribosome Shunt on the Cauliflower Mosaic Virus RNA Leader

Journal of Biological Chemistry ◽

10.1074/jbc.m001143200 ◽

2000 ◽

Vol 275 (23) ◽

pp. 17288-17296 ◽

Cited By ~ 34

Author(s):

Mikhail M. Pooggin ◽

Thomas Hohn ◽

Johannes Fütterer

Keyword(s):

Mosaic Virus ◽

Cauliflower Mosaic Virus ◽

Open Reading Frame ◽

Reading Frame ◽

Virus Rna ◽

Short Open Reading Frame

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Multiple proteins and subgenomic mRNAs may be derived from a single open reading frame on tobacco mosaic virus RNA

Nucleic Acids Research ◽

10.1093/nar/11.3.801 ◽

1983 ◽

Vol 11 (3) ◽

pp. 801-821 ◽

Cited By ~ 25

Author(s):

Tony Hunter ◽

Richard Jackson ◽

David Zimmern

Keyword(s):

Tobacco Mosaic Virus ◽

Mosaic Virus ◽

Open Reading Frame ◽

Single Open Reading Frame ◽

Reading Frame ◽

Virus Rna

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Sequence and expression of the dCMP deaminase gene (DCD1) of Saccharomyces cerevisiae

Molecular and Cellular Biology ◽

10.1128/mcb.6.5.1711-1721.1986 ◽

1986 ◽

Vol 6 (5) ◽

pp. 1711-1721

Author(s):

E M McIntosh ◽

R H Haynes

Keyword(s):

Saccharomyces Cerevisiae ◽

Amino Acids ◽

Amino Acid ◽

Amino Acid Sequences ◽

Open Reading Frame ◽

Northern Analysis ◽

Hindiii Site ◽

Reading Frame ◽

Hindiii Restriction Site ◽

Cycle Dependent

The dCMP deaminase gene (DCD1) of Saccharomyces cerevisiae has been isolated by screening a Sau3A clone bank for complementation of the dUMP auxotrophy exhibited by dcd1 dmp1 haploids. Plasmid pDC3, containing a 7-kilobase (kb) Sau3A insert, restores dCMP deaminase activity to dcd1 mutants and leads to an average 17.5-fold overproduction of the enzyme in wild-type cells. The complementing activity of the plasmid was localized to a 4.2-kb PvuII restriction fragment within the Sau3A insert. Subcloning experiments demonstrated that a single HindIII restriction site within this fragment lies within the DCD1 gene. Subsequent DNA sequence analysis revealed a 936-nucleotide open reading frame encompassing this HindIII site. Disruption of the open reading frame by integrative transformation led to a loss of enzyme activity and confirmed that this region constitutes the dCMP deaminase gene. Northern analysis indicated that the DCD1 mRNA is a 1.15-kb poly(A)+ transcript. The 5' end of the transcript was mapped by primer extension and appears to exhibit heterogeneous termini. Comparison of the amino acid sequence of the T2 bacteriophage dCMP deaminase with that deduced for the yeast enzyme revealed a limited degree of homology which extends over the entire length of the phage polypeptide (188 amino acids) but is confined to the carboxy-terminal half of the yeast protein (312 amino acids). A potential dTTP-binding site in the yeast and phage enzymes was identified by comparison of homologous regions with the amino acid sequences of a variety of other dTTP-binding enzymes. Despite the role of dCMP deaminase in dTTP biosynthesis, Northern analysis revealed that the DCD1 gene is not subject to the same cell cycle-dependent pattern of transcription recently found for the yeast thymidylate synthetase gene (TMP1).

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Inhibition of alfalfa mosaic virus RNA and protein synthesis byactinomycin D and cycloheximide

Virology ◽

10.1016/s0042-6822(83)80009-9 ◽

1983 ◽

Vol 126 (2) ◽

pp. 517-524 ◽

Cited By ~ 9

Author(s):

Annette Nassuth ◽

Fieke Alblas ◽

Ad J.M. Van Der Geest ◽

John F. Bol

Keyword(s):

Protein Synthesis ◽

Mosaic Virus ◽

Alfalfa Mosaic Virus ◽

Virus Rna ◽

Rna And Protein Synthesis

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Yeast Lsm1p-7p/Pat1p Deadenylation-Dependent mRNA-Decapping Factors Are Required for Brome Mosaic Virus Genomic RNA Translation

Molecular and Cellular Biology ◽

10.1128/mcb.23.12.4094-4106.2003 ◽

2003 ◽

Vol 23 (12) ◽

pp. 4094-4106 ◽

Cited By ~ 70

Author(s):

Amine O. Noueiry ◽

Juana Diez ◽

Shaun P. Falk ◽

Jianbo Chen ◽

Paul Ahlquist

Keyword(s):

Mosaic Virus ◽

Rna Replication ◽

Brome Mosaic Virus ◽

Open Reading Frame ◽

Viral Rna ◽

Genomic Rna ◽

Reading Frame ◽

Mrna Decapping ◽

Rna Translation ◽

Positive Strand Rna

ABSTRACT Previously, we used the ability of the higher eukaryotic positive-strand RNA virus brome mosaic virus (BMV) to replicate in yeast to show that the yeast LSM1 gene is required for recruiting BMV RNA from translation to replication. Here we extend this observation to show that Lsm1p and other components of the Lsm1p-Lsm7p/Pat1p deadenylation-dependent mRNA decapping complex were also required for translating BMV RNAs. Inhibition of BMV RNA translation was selective, with no effect on general cellular translation. We show that viral genomic RNAs suitable for RNA replication were already distinguished from nonreplication templates at translation, well before RNA recruitment to replication. Among mRNA turnover pathways, only factors specific for deadenylated mRNA decapping were required for BMV RNA translation. Dependence on these factors was not only a consequence of the nonpolyadenylated nature of BMV RNAs but also involved the combined effects of the viral 5′ and 3′ noncoding regions and 2a polymerase open reading frame. High-resolution sucrose density gradient analysis showed that, while mutating factors in the Lsm1p-7p/Pat1p complex completely inhibited viral RNA translation, the levels of viral RNA associated with ribosomes were only slightly reduced in mutant yeast. This polysome association was further verified by using a conditional allele of essential translation initiation factor PRT1, which markedly decreased polysome association of viral genomic RNA in the presence or absence of an LSM7 mutation. Together, these results show that a defective Lsm1p-7p/Pat1p complex inhibits BMV RNA translation primarily by stalling or slowing the elongation of ribosomes along the viral open reading frame. Thus, factors in the Lsm1p-7p/Pat1p complex function not only in mRNA decapping but also in translation, and both translation and recruitment of BMV RNAs to viral RNA replication are regulated by a cell pathway that transfers mRNAs from translation to degradation.

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Nucleotide and Amino Acid Sequences of the Metallo-β-Lactamase, ImiS, from Aeromonas veronii bv. sobria

Antimicrobial Agents and Chemotherapy ◽

10.1128/aac.42.2.436 ◽

1998 ◽

Vol 42 (2) ◽

pp. 436-439 ◽

Cited By ~ 22

Author(s):

T. R. Walsh ◽

W. A. Neville ◽

M. H. Haran ◽

D. Tolson ◽

D. J. Payne ◽

...

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Active Site ◽

Amino Acid Sequences ◽

Open Reading Frame ◽

Reading Frame ◽

Aeromonas Veronii ◽

Putative Active Site ◽

Lactamase Gene ◽

Active Site Sequence

ABSTRACT The Aeromonas veronii bv. sobria metallo-β-lactamase gene, imiS, was cloned. The imiS open reading frame extends for 762 bp and encodes a protein of 254 amino acids with a secreted modified protein of 227 amino acids and a predicted pI of 8.1. To confirm the predicted sequence, purified ImiS was digested and the resulting peptides were identified, yielding an identical sequence for ImiS, with 98% identity to CphA. Both possessed the putative active-site sequence Asn-Tyr-His-Thr-Asp at positions 88 to 92, which is unique to the Aeromonas metallo-β-lactamases.

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