کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
11019569 | 1717633 | 2019 | 26 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Purification and functional characterization of tomato mosaic virus 130K protein expressed in silkworm pupae using a baculovirus vector
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موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Tomato mosaic virus (ToMV; genus, Tobamovirus) is a member of the alpha-like virus superfamily of positive-strand RNA viruses, which includes many plant and animal viruses of agronomical and clinical importance. The genomes of alpha-like viruses encode replication-associated proteins that contain methyltransferase, helicase and/or polymerase domains. The three-dimensional structure of the helicase domain fragment of ToMV has been determined, but the structures of the other domains of alpha-like virus replication proteins are not available. In this study, we expressed full-length ToMV replication-associated protein 130â¯K, which contains the methyltransferase and helicase domains, using the baculovirus-silkworm expression system and purified the recombinant protein to near homogeneity. Purified 130â¯K, which was stable in phosphate buffer containing magnesium ions and ATP, formed a dimer in solution and hydrolyzed nucleoside 5â²-triphosphates.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Protein Expression and Purification - Volume 154, February 2019, Pages 85-90
Journal: Protein Expression and Purification - Volume 154, February 2019, Pages 85-90
نویسندگان
Chihoko Kobayashi, Masahiko Kato, Hidekazu Nagaya, Nobutaka Shimizu, Kazuhiro Ishibashi, Masayuki Ishikawa, Etsuko Katoh,