Self-assembly of the bacterial cytoskeleton-associated RNA helicase B protein into polymeric filamentous structures.
The Escherichia coli RNA degradosome proteins are organized into a helical cytoskeletal-like structure within the cell. Here we describe the ATP-dependent assembly of the RhlB component of the degradosome into polymeric filamentous structures in vitro, which suggests that extended polymers of RhlB are likely to comprise a basic core element of the degradosome cytoskeletal structures.
Taghbalout
Aziz
A
Department of Molecular, Microbial, and Structural Biology, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, CT 06032, USA. taghbalout@neuron.uchc.edu
Yang
Qingfen
Q
D000255:Adenosine Triphosphate / Q000378:metabolism; D003599:Cytoskeleton / Q000378:metabolism*; D053487:DEAD-box RNA Helicases / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial / Q000502:physiology; D007150:Immunohistochemistry; D021381:Protein Transport
D029968:Escherichia coli Proteins; D000255:Adenosine Triphosphate; C502431:RhlB protein, E coli; D053487:DEAD-box RNA Helicases
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