RNA Helicases

Fuller-Pace, FV; Lane, David P.

doi:10.1007/978-3-642-77356-3_9

Cited by 5 publications

(3 citation statements)

References 42 publications

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“…DEAD/H proteins are defined by seven conserved motifs that are required for ATP binding and hydrolysis and RNA unwinding (Gorbalenya and Koonin, 1993; Fuller‐Pace, 1994). Most DEAD/H proteins also contain unique N‐ and/or C‐terminal extensions that may mediate their interactions with other proteins or specific RNA sequences (Fuller‐Pace and Lane, 1992; Wang and Guthrie, 1998). In vivo , DEAD/H proteins are found generally as members of large multiprotein complexes and often act to rearrange a single RNA helix in a complex pathway.…”

Section: Introductionmentioning

confidence: 99%

Escherichia coli DbpA is an RNA helicase that requires hairpin 92 of 23S rRNA

2001

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Escherichia coli DbpA is a member of the DEAD/H family of proteins which has been shown to have robust ATPase activity only in the presence of a specific region of 23S rRNA. A series of bimolecular RNA substrates were designed based on this activating region of rRNA and used to demonstrate that DbpA is also a non-processive, sequence-specific RNA helicase. The high affinity of DbpA for the RNA substrates allowed both single and multiple turnover helicase assays to be performed. Helicase activity of DbpA is dependent on the presence of ATP or dATP, the sequence of the loop of hairpin 92 of 23S rRNA and the position of the substrate helix with respect to hairpin 92. This work indicates that certain RNA helicases require particular RNA structures in order for optimal unwinding activity to be observed.

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Section: Introductionmentioning

confidence: 99%

Escherichia coli DbpA is an RNA helicase that requires hairpin 92 of 23S rRNA

2001

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“…DEAD box proteins are found in a wide range of organisms, ranging from bacteria to mammals, and are involved in a variety of processes such as ribosome assembly, initiation of translation, mRNA splicing, and development (2,3). Multiple DEAD box proteins have been identified in organisms with small genomes [e.g., 20 in yeast (5) and 5 in Escherichia coli (6)], suggesting that they have specific functions that require interaction with specific RNA substrates.…”

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confidence: 99%

“…DbpA is a member of the large "DEAD box" family of putative RNA helicases, so called because they share the highly conserved motif Asp-Glu-Ala-Asp together with several other conserved functional elements (1)(2)(3)(4). DEAD box proteins are found in a wide range of organisms, ranging from bacteria to mammals, and are involved in a variety of processes such as ribosome assembly, initiation of translation, mRNA splicing, and development (2,3).…”

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confidence: 99%

The "DEAD box" protein DbpA interacts specifically with the peptidyltransferase center in 23S rRNA.

Nicol

Fuller-Pace

1995

Proc. Natl. Acad. Sci. U.S.A.

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The Escherichia coli DEAD (Asp-Glu-AlaAsp) box protein DbpA is a putative RNA helicase and established RNA-dependent ATPase and is the only member of the DEAD box protein family for which a specific RNA substrate, bacterial 23S rRNA, has been identified. We have investigated the nature of this specificity in depth and have localized by deletion mutagenesis and PCR a single region of 93 bases (bases 2496-2588) in 23S rRNA that is both necessary and sufficient for complete activation of ATPase activity of DbpA. This target region forms part of the peptidyltransferase center and includes many bases involved in interaction with the 3' terminal adenosines of both A-and P-site tRNAs. Deletion of stem loops within the 93-base segment abolished ATPase activation. Similarly, point mutations that disrupt base pairing within stem structures ablated stimulation of ATPase activity. These data are consistent with roles for DbpA either in establishing and/or maintaining the correct threedimensional structure of the peptidyltransferase center in 23S rRNA during ribosome assembly or in the peptidyltransferase reaction.DbpA is a member of the large "DEAD box" family of putative RNA helicases, so called because they share the highly conserved motif Asp-Glu-Ala-Asp together with several other conserved functional elements (1-4). DEAD box proteins are found in a wide range of organisms, ranging from bacteria to mammals, and are involved in a variety of processes such as ribosome assembly, initiation of translation, mRNA splicing, and development (2, 3). Multiple DEAD box proteins have been identified in organisms with small genomes [e.g., 20 in yeast (5) and 5 in Escherichia coli (6)], suggesting that they have specific functions that require interaction with specific RNA substrates. Individual members of the DEAD box family are highly conserved, and many are required for viability (7), implying that they perform essential functions in the cell. These proteins are thought to be involved in the local unwinding of RNA secondary structures in a variety of biological processes and may, therefore, play a role in maintaining the optimal conformation of these RNA molecules or in regulating the biological events in which they are involved through controlling RNA structure.The E. coli dbpA gene was originally isolated by hybridization with a probe from the Saccharomyces pombe homolog of p68, one of the prototypic DEAD box proteins (8). However, DbpA is no more related to p68 than to any other members of the DEAD box family. To date, five DEAD box protein genes have been reported in E. coli. Apart from dbpA (8), these include srmB (9) and deaD (10) which, when expressed at high-copy number, will suppress the effect of temperaturesensitive lethal mutations in L24 and S2, respectively, suggesting a role in ribosome biogenesis. Another gene, rhlB, appears essential only in some genetic backgrounds (6), but conditionalThe publication costs of this article were defrayed in part by page charge payment. This articl.-must therefore be hereby ...

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