Nucleotide sequence of the 3′ half of zucchini yellow mosaic virus (Singapore isolate) genome encoding the 4K protein, protease, polymerase and coat protein

Wu, Mian; Yeong, Ching-Yuen; Wong, Sek‐Man

doi:10.1093/nar/21.5.1317

Cited by 7 publications

(1 citation statement)

References 2 publications

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“…The elucidation of the structure of such virus-encoded proteins could eventually facilitate the design of novel polypeptides which bind to them and inhibit their functions. With this objective, cDNAs for NIa proteases were cloned and sequenced from bean yellow mosaic virus (22) and zucchini yellow mosaic virus (Singapore isolate) (316).…”

Section: Virusesmentioning

confidence: 99%

Molecular and Biotechnological Aspects of Microbial Proteases

Rao

Tanksale

Ghatge

et al. 1998

Microbiol Mol Biol Rev

1,766

721

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SUMMARY Proteases represent the class of enzymes which occupy a pivotal position with respect to their physiological roles as well as their commercial applications. They perform both degradative and synthetic functions. Since they are physiologically necessary for living organisms, proteases occur ubiquitously in a wide diversity of sources such as plants, animals, and microorganisms. Microbes are an attractive source of proteases owing to the limited space required for their cultivation and their ready susceptibility to genetic manipulation. Proteases are divided into exo- and endopeptidases based on their action at or away from the termini, respectively. They are also classified as serine proteases, aspartic proteases, cysteine proteases, and metalloproteases depending on the nature of the functional group at the active site. Proteases play a critical role in many physiological and pathophysiological processes. Based on their classification, four different types of catalytic mechanisms are operative. Proteases find extensive applications in the food and dairy industries. Alkaline proteases hold a great potential for application in the detergent and leather industries due to the increasing trend to develop environmentally friendly technologies. There is a renaissance of interest in using proteolytic enzymes as targets for developing therapeutic agents. Protease genes from several bacteria, fungi, and viruses have been cloned and sequenced with the prime aims of (i) overproduction of the enzyme by gene amplification, (ii) delineation of the role of the enzyme in pathogenecity, and (iii) alteration in enzyme properties to suit its commercial application. Protein engineering techniques have been exploited to obtain proteases which show unique specificity and/or enhanced stability at high temperature or pH or in the presence of detergents and to understand the structure-function relationships of the enzyme. Protein sequences of acidic, alkaline, and neutral proteases from diverse origins have been analyzed with the aim of studying their evolutionary relationships. Despite the extensive research on several aspects of proteases, there is a paucity of knowledge about the roles that govern the diverse specificity of these enzymes. Deciphering these secrets would enable us to exploit proteases for their applications in biotechnology.

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Section: Virusesmentioning

confidence: 99%

Molecular and Biotechnological Aspects of Microbial Proteases

Rao

Tanksale

Ghatge

et al. 1998

Microbiol Mol Biol Rev

1,766

721

View full text Add to dashboard Cite

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Sequence variability within the 3′-proximal part of the Sweet potato mild mottle virus genome

2003

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Sweet potato mild mottle virus (SPMMV) is the type member of the genus Ipomovirus (family Potyviridae) and is only known to occur in East Africa. In Uganda, SPMMV is the third most prevalent virus infecting sweet potato. The sequence variability of SPMMV was studied by cloning and sequencing a 1.8-kb fragment representing the 3'-end of the genome of eight SPMMV isolates collected from different districts of Uganda. Sequence comparisons indicated 85.9-99.9% nucleotide sequence identity and 92.8-100% amino acid sequence similarity for the coat protein (CP) encoding region. The nucleotide sequence identity within the 3'-untranslated region (3' UTR) was 84.7-100%, and the region was variable in length (303-308 nucleotides) due to some deletions within the 5'-proximal part of the 3' UTR. Phylogenetic analysis of the CP amino acid sequences revealed significant clustering, indicating the existence of distinguishable sequence variants or strains. The low CP amino acid sequence similarity of SPMMV isolates with other characterised viruses of the family Potyviridae and the unusual putative proteolytic cleavage site at the NIb/CP junction further demonstrate SPMMV as a very distinct virus in the family Potyviridae.

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Identification of Zucchini yellow mosaic potyvirus by RT-PCR and analysis of sequence variability

Thomson

Dietzgen

Gibbs

et al. 1995

Journal of Virological Methods

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Nucleotide sequence of the 3′ half of zucchini yellow mosaic virus (Singapore isolate) genome encoding the 4K protein, protease, polymerase and coat protein

Abstract: A single open reading frame (ORF) of 3870 nucleotide sequence of the 3' half of ZYMV-S (1) was determined from a cDNA

Cited by 7 publications

References 2 publications

Molecular and Biotechnological Aspects of Microbial Proteases

Molecular and Biotechnological Aspects of Microbial Proteases

Sequence variability within the 3′-proximal part of the Sweet potato mild mottle virus genome

Identification of Zucchini yellow mosaic potyvirus by RT-PCR and analysis of sequence variability

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