Literature summary for 3.6.4.13 extracted from

Wang, X.; Lee, W.M.; Watanabe, T.; Schwartz, M.; Janda, M.; Ahlquist, P.
Brome mosaic virus 1a nucleoside triphosphatase/helicase domain plays crucial roles in recruiting RNA replication templates (2005), J. Virol., 79, 13747-13758.

Search for more literature for 3.6.4.13

Cloned(Commentary)

Cloned (Comment)	Organism
expression of GST-fusion wild-type and mutant enzymes in Escherichia coli strain C41(DE3)	Brome mosaic virus

Protein Variants

Protein Variants	Comment	Organism
D755A	site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 90% reduced ATPase activity compared to the wild-type enzyme	Brome mosaic virus
F788A	site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 30% reduced ATPase activity compared to the wild-type enzyme	Brome mosaic virus
G781S	site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 75% reduced ATPase activity compared to the wild-type enzyme	Brome mosaic virus
H903A	site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 45% reduced ATPase activity compared to the wild-type enzyme	Brome mosaic virus
K691A	site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 80% reduced ATPase activity compared to the wild-type enzyme	Brome mosaic virus
additional information	trans interference by BMV 1a protein helicase mutants with BMV 1a protein-stimulated RNA3 accumulation, overview	Brome mosaic virus
Q785A	site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 65% reduced ATPase activity compared to the wild-type enzyme	Brome mosaic virus
Q785E	site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 75% reduced ATPase activity compared to the wild-type enzyme	Brome mosaic virus
R791A	site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 10% increased ATPase activity compared to the wild-type enzyme	Brome mosaic virus
R815L	site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 60% increased ATPase activity compared to the wild-type enzyme	Brome mosaic virus
R938A	site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 45% reduced ATPase activity compared to the wild-type enzyme	Brome mosaic virus
S790A	site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 60% reduced ATPase activity compared to the wild-type enzyme	Brome mosaic virus
S790W	site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 70% reduced ATPase activity compared to the wild-type enzyme	Brome mosaic virus
T812A/Y813A	site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows unaltered ATPase activity compared to the wild-type enzyme	Brome mosaic virus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
additional information	BMV 1a protein accumulates on endoplasmic reticulum membranes of the host cell	Brome mosaic virus	-	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required for ATPase activity	Brome mosaic virus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + H2O	Brome mosaic virus	NTPase activity	ADP + phosphate	-	?
additional information	Brome mosaic virus	BMV 1a protein accumulates on endoplasmic reticulum membranes of the host cell, recruits the other RNA replication factor 2apol and induces 50- to 70-nm membrane invaginations serving as RNA replication compartments, BMV 1a protein also recruits viral replication templates such as genomic RNA3 depending on the BMV 1a protein helicase motif, in absence of 2apol, BMV 1a protein highly stabilizes RNA3 by transferring it to a membrane-associated, nuclease-resistant state, overview	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Brome mosaic virus	-	i.e. BMV	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant GST-fusion wild-type and mutant enzymes from Escherichia coli strain C41(DE3) by glutathione affinity chromatography	Brome mosaic virus

Source Tissue

Source Tissue	Comment	Organism	Textmining
additional information	the virus is propagated in yeast cells	Brome mosaic virus	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	RNA replication, RNA protection, spherule formation size, relative ATPase activity, RNA accumulation and stabilization, of wild-type and mutant enzymes, overview	Brome mosaic virus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O	NTPase activity	Brome mosaic virus	ADP + phosphate	-	?
additional information	BMV 1a protein accumulates on endoplasmic reticulum membranes of the host cell, recruits the other RNA replication factor 2apol and induces 50- to 70-nm membrane invaginations serving as RNA replication compartments, BMV 1a protein also recruits viral replication templates such as genomic RNA3 depending on the BMV 1a protein helicase motif, in absence of 2apol, BMV 1a protein highly stabilizes RNA3 by transferring it to a membrane-associated, nuclease-resistant state, overview	Brome mosaic virus	?	-	?
additional information	multifunctional enzyme showing protease, helicase, and NTPase activities, the enzyme has a function in RNA replication complex assembly besides its function in RNA synthesis/capping, the enzyme activity is located in the C-terminal nucleoside triphosphatase/helicase domain of the BMV 1a protein RNA replication factor	Brome mosaic virus	?	-	?

Subunits

Subunits	Comment	Organism
More	the enzyme activity is located in the C-terminal nucleoside triphosphatase/helicase domain of the BMV 1a protein RNA replication factor, BMV 1a protein contains an N-terminal capping domain with m7G-methyltransferase and m7GMP binding activities, and a C-terminal NTPase/helicase-like domain, comprising residues 562-961, containing 7 conserved helicase motifs, the two domains are separated by a proline-rich region, overview	Brome mosaic virus

Synonyms

Synonyms	Comment	Organism
1a NTPase/helicase	-	Brome mosaic virus
BMV 1a protein	-	Brome mosaic virus
nucleoside triphosphatase/helicase	-	Brome mosaic virus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	ATPase assay at	Brome mosaic virus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.4	-	ATPase assay at	Brome mosaic virus

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Release 2023.1 (January 2023)