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1 unlikely to be extensively folded within the degradosome.
2 lytic "machine" that has been termed the RNA degradosome.
3 3'-exoribonuclease and component of the RNA degradosome.
4 nd for the regeneration of ATP by PPK in the degradosome.
5 d RhlB are two other major components of the degradosome.
6 r the organization and mechanisms of the RNA degradosome.
7 exoribonuclease, DSS1, to function as an RNA degradosome.
8 ate the destruction of such RNAs by the mRNA degradosome.
9 for the complex to serve as an effective RNA degradosome.
10 rapid decay possibly facilitated by the mRNA degradosome.
11 ode of action, and its assembly into the RNA degradosome.
12 rganizes the other protein components of the degradosome.
13 ll-sized mRNAs at (UUC)n runs by the E. coli degradosome.
14 of a large RNA-catalysis machine termed the degradosome.
15 er proteins to form a complex termed the RNA degradosome.
16 arget specific classes of mRNAs for decay by degradosomes.
17 - a major component of E. coli RNase E-based degradosomes.
18 erties of recombinant and cell-extracted RNA degradosomes.
19 s into the structure and dynamics of the RNA degradosome, a fascinating and complex macromolecular as
20 the carboxy-terminal half organizes the RNA degradosome, a multi-enzyme complex that degrades mRNA c
21 ) is a component of the Escherichia coli RNA degradosome, a multiprotein complex that also includes R
22 that the functional requirements of SUV3 for degradosome activity and maintenance of mtDNA stability
25 ized RNase RnpA interacts with the S. aureus degradosome and that this interaction is conserved in ot
26 ffecting both the protein composition of the degradosome and the endonucleolytic activity of RNase E.
29 We conclude that the constituents of the RNA degradosome are components of the E. coli cytoskeleton,
31 he principal components of the C. crescentus degradosome are the endoribonuclease RNase E, the exorib
32 the isolation and characterization of an RNA degradosome assembly from the alpha-proteobacterium Caul
35 many bacterial species, the multi-enzyme RNA degradosome assembly makes key contributions to RNA meta
36 e RhlB is a component of the multienzyme RNA degradosome assembly, and its interaction with the core
41 tial and stationary phases and find that the degradosome can contain up to 10 different proteins unde
42 and RNA helicase B (RhlB) components of the degradosome can each independently form coiled structure
45 s a scaffold for formation of a multiprotein degradosome complex modulates the inhibition of RNase E
46 gulation of manX did not require the RNase E degradosome complex, suggesting that the primary mechani
47 r their 5'-end and is a component of the RNA degradosome complex, which also contains the 3'-exonucle
51 udies showed that RNaseE and the other known degradosome components (RNA helicase B, polynucleotide p
52 ted in vitro the binary interactions between degradosome components and have characterized interactio
54 ng proteins that modulate the remodelling of degradosome composition in bacteria and argue that such
55 distinct, and inhibitor-specific changes in degradosome composition--and that these are in turn asso
57 lution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phospho
58 ins, affected differentially by mutations in degradosome constituents, or not detectably altered by d
60 evidence that PAP I interacts with the mRNA degradosome during both exponential and stationary phase
62 nsuspected effects of RNase E deficiency and degradosome formation on nutrient utilization by E. coli
63 lyses to an E. coli strain with impaired RNA degradosome formation, we investigated the biological co
64 eveloped a procedure to reconstitute the RNA degradosome from recombinant components using modular co
69 processing of structural precursors, the RNA degradosome has differential activities on a spectrum of
71 ll-length RNase E, which allows formation of degradosomes, have nutritional requirements different fr
74 mily and for the assembly of the E. coli RNA degradosome, in which RNase E is the central component.
76 endent assembly of the RhlB component of the degradosome into polymeric filamentous structures in vit
84 s the fact that the presence of a functional degradosome is essential for RNase E to detect increased
86 Here we demonstrate that the RNase E-based degradosome is required for poly(A) polymerase I (PAP I)
87 that of the core complex of the E. coli RNA degradosome lacking RNase E but very different from that
89 Recent studies have provided evidence for a degradosome-like complex inB. subtilisthat is built arou
90 sis identified the Staphylococcus aureus RNA degradosome-like complex to include RNase J1, RNase J2,
91 matic activity, and suggest the existence of degradosome-like complexes in Gram-positive bacteria.
92 that enolase is recruited into putative RNA degradosome machinery in these bacilli, where it plays c
93 ts indicate that RNase E associated with the degradosome may contribute to the removal of poly(A) tai
95 y located within the coding sequences in the degradosome mutants compared to the wild type control wh
98 component of the Pseudomonas aeruginosa RNA degradosome, occluding them from substrates and resultin
101 here that the assembly of the RNase E-based degradosome of Escherichia coli is not required for norm
102 RNaseE is the main component of the RNA degradosome of Escherichia coli, which plays an essentia
103 inct from those found in proteobacteria, the degradosomes of which are assembled around the unstructu
104 n of PNPase because association with the RNA degradosome or with RNA helicase B (RhlB) is not require
105 icing through RNA degradation as part of the degradosome, or has a direct role in splicing as a chape
106 donuclease RNase E and components of the RNA degradosome, particularly enolase, a glycolytic enzyme w
108 , we identify an additional component of the degradosome, polyphosphate kinase (PPK), which catalyses
111 degradosomes, whereas others are acted on by degradosome proteins functioning independently of the co
112 , the cytoskeletal organization of the other degradosome proteins required the presence of the RNaseE
113 ndance were affected congruently by multiple degradosome proteins, affected differentially by mutatio
116 composition in bacteria and argue that such degradosome remodelling is a mechanism for the different
124 he rates of capture of the limited number of degradosomes, so that they become recruited to sites of
125 bic conditions, enolase bound to the RNase E/degradosome stabilizes the small RNA (sRNA) DicF, i.e.,
127 nent ribonucleolytic complexes known as "RNA degradosomes." These complexes consist of four major com
128 to a multi-enzyme assembly, known as the RNA degradosome, through an interaction with the scaffolding
129 of the ribonucleolytic activities within the degradosome to 3' attack since previous studies had only
130 t that polyadenylation requires a functional degradosome to maintain an equilibrium between free PNPa
132 mechanism by which Ecoli uses enolase-bound degradosomes to switch from rod-shaped to filamentous fo
133 processing and degradative activities of the degradosome, to regulate their access to important cellu
134 port that presence of enolase in the RNase E/degradosome under anaerobic conditions regulates cell mo
135 ctive PNPase protein that still forms intact degradosomes, we show that a catalytically active PNPase
136 s in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome
137 is a critical component of the mitochondrial degradosome, which also includes a 3' --> 5' exonuclease
138 tic enzyme enolase is a component of the RNA degradosome, which is an RNase E mediated assembly invol
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