The 42-kDa coat protein of Andean potato mottle virus acts as a transcriptional activator in yeast

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The 42-kDa coat protein of Andean potato mottle virus acts as a transcriptional activator in yeast.

Interactions of viral proteins play an important role in the virus life cycle, especially in capsid assembly. Andean potato mottle comovirus (APMoV) is a plant RNA virus with a virion formed by two coat proteins (CP42 and CP22). Both APMoV coat protein open reading frames were cloned into pGBT9 and pGAD10, two-hybrid system vectors. HF7c yeast cells transformed with the p9CP42 construct grew on...

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Molecular cloning and sequence analysis of an andean potato mottle virus cDNA clone encoding the major coat protein.

Departamento de Genetica, Universidade Federal do Rio de Janeiro, CP 6801 1, CEP 21944, Rio de Janeiro, Brasil (N.S., R.K., D.E.d.O.); Departamento de Fitopatologia, Universidade Federal Rural do Rio de Janeiro, CP 23851, Rio de Janeiro, Brasil (P.S.T.B.); Departamento de Genetica, Fundagco Oswaldo Cruz, CP 926, Rio de laneiro, Brasil (A.C.P.V.); Departamento de Bioquimica, Universidade Federal...

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Heterologous Expression of Potato Virus Y Coat Protein, Isolate Pot187

Background: The advent of recombinant DNA technology has facilitated heterologous expression of proteins from various sources in different host systems including Escherichia coli. If a plant virus coat protein is expressed in the bacterium it can be used as the antigen for antibody preparation. Such a recombinant antigen preparation can be particularly useful where equipment such as ultracentri...

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Rpm2p, a component of yeast mitochondrial RNase P, acts as a transcriptional activator in the nucleus.

Rpm2p, a protein subunit of yeast mitochondrial RNase P, has another function that is essential in cells lacking the wild-type mitochondrial genome. This function does not require the mitochondrial leader sequence and appears to affect transcription of nuclear genes. Rpm2p expressed as a fusion protein with green fluorescent protein localizes to the nucleus and activates transcription from prom...

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Primary structure of belladonna mottle virus coat protein.

The coat protein of belladonna mottle virus (a tymovirus) was cleaved by trypsin and chymotrypsin, and the peptides were separated by high performance liquid chromatography using a combination of gel permeation, reverse phase, and ion pair chromatography. The peptides were sequenced manually using the 4-N, N-dimethylaminoazobenzene-4'-isothiocyanate/phenyl isothiocyanate double-coupling method....

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ژورنال

عنوان ژورنال: Brazilian Journal of Medical and Biological Research

سال: 2002

ISSN: 0100-879X

DOI: 10.1590/s0100-879x2002000400001