Regulation of the <i>Escherichia coli uncH</i> gene by mRNA secondary structure and translational coupling

Pati, Sushma; DiSilvestre, Deborah; Brusilow, William S.A.

doi:10.1111/j.1365-2958.1992.tb01791.x

Cited by 15 publications

(9 citation statements)

References 30 publications

(20 reference statements)

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“…The different subunits of E. coli ATP synthase are translated from a polycistronic atp mRNA, and a balanced stoichiometry is obtained by translational coupling between the cistrons as well as regulation by mRNA secondary structure (14,15). In most bacteria, the cistrons are arranged in clusters separating those for F O from those for F 1 , an arrangement fitting well with the proposal that both have been evolved from functionally unrelated ancestor protein complexes (16 -18).…”

mentioning

confidence: 51%

Subunit δ Is the Key Player for Assembly of the H+-translocating Unit of Escherichia coli FOF1 ATP Synthase

Hilbers¹,

Eggers²,

Pradela

et al. 2013

Journal of Biological Chemistry

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mentioning

confidence: 51%

Subunit δ Is the Key Player for Assembly of the H+-translocating Unit of Escherichia coli FOF1 ATP Synthase

Hilbers¹,

Eggers²,

Pradela

et al. 2013

Journal of Biological Chemistry

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“…2 Two factors that may have contributed to this low expression were corrected in the construction of pJC1. First, evidence that an mRNA secondary structure encompassing the region of uncH from the ShineDalgarno to residue 36 of the coding sequence strongly reduces expression has been presented by Pati and co-workers (47). In the construction of plasmid pJC1, the expression cassette polymerase chain reaction strategy of MacFerrin et al (38) was used to replace C and G residues in the spacer region between the Shine-Dalgarno and the initiation codon with A or T to weaken this secondary structure, making the translation initiation region more accessible to ribosomes.…”

Section: Resultsmentioning

confidence: 99%

Characterization of a b2δ Complex fromEscherichia coli ATP Synthase

Dunn

Chandler

1998

Journal of Biological Chemistry

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The proton-translocating ATP synthases couple the generation of ATP to the protonmotive force present across membranes involved in energy transduction (for reviews, see Refs. 1-4). These complex enzymes consist of a peripheral F 1 sector, which catalyzes ATP synthesis and hydrolysis, and an integral F 0 sector, which catalyzes movements of protons across the membrane. In the relatively simple ATP synthase of Escherichia coli, F 1 contains five types of subunits in a stoichiometry of ␣ 3 ␤ 3 ␥␦⑀, while F 0 contains three types of subunits in a stoichiometry of ab 2 c 9 -12 . Subunit interactions at the interface of the two sectors are responsible for coupling their catalytic activities.Recent work has strongly indicated that hydrolysis of ATP by F 1 is accompanied by rotation of the ␥ and ⑀ subunits relative to the ␣ 3 ␤ 3 hexameric ring (5-11), consistent with proposals from Paul Boyer's laboratory (12). The high resolution structure of the mitochondrial F 1 (13) reveals that the N and C termini of ␥ form an antiparallel coiled-coil running up the center of the ␣ 3 ␤ 3 ring; this structure appears to function as an asymmetric spindle, which, by rotating, plays the major role in directing conformational changes at the catalytic sites. In the intact ATP synthase, the rotation of ␥ and ⑀ should be coupled to proton conduction through F 0 . The a and c subunits provide those residues that are essential for proton conduction.In all systems, ␦ or the analogous mitochondrial protein called oligomycin sensitivity conferral protein (OSCP), 1 is essential for the coupling of the catalytic activities of the two sectors. The ␦ subunit (reviewed in Ref. 14) has no significant effect on steady-state ATP hydrolysis rates by isolated F 1 -ATPase but does alter unisite hydrolysis (15). ␦ binds to F 1 through interactions with the external surface of the N-terminal third of the ␣ subunit (16 -20). In some systems, ␦ alters the proton permeability of F 0 (21). This effect is not seen in E. coli, but here ␦ is essential for the interaction of F 1 and F 0 , implying a link between ␦ and F 0 (22). The physical and functional nature of the ␦-F 0 interaction is currently the subject of intense interest. In recent work, an interaction of ␦ or OSCP with the b subunit of F 0 has been demonstrated (23-25). Nearest neighbor analysis by chemical cross-linking had not revealed crosslinks between b and ␦ in the E. coli system (26), but they had been reported for the corresponding subunits in the chloroplast (27) and mitochondrial (28) enzymes. The importance of the cytoplasmic domain of b to the F 1 -F 0 interaction has also been demonstrated through proteolysis (29 -31) and direct binding (32) studies.E. coli ␦ purified following pyridine treatment of F 1 -ATPase was shown to be an elongated monomer (33), but the low yield of the preparation limited the scope of work that could be carried out. The current studies were undertaken to produce recombinant ␦ in quantities appropriate for high resolution structural analysis and to permit the charac...

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“…For many RNA molecules, the right secondary structure is a prerequisite for their function. This is well known for secondary structure elements of messenger RNAs, and for the genomes of RNA viruses [38–46]. It means two things.…”

Section: A Different Perspective On Neutralitymentioning

confidence: 99%

Robustness, evolvability, and neutrality

2005

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Biological systems, from macromolecules to whole organisms, are robust if they continue to function, survive, or reproduce when faced with mutations, environmental change, and internal noise. I focus here on biological systems that are robust to mutations and ask whether such systems are more or less evolvable, in the sense that they can acquire novel properties. The more robust a system is, the more mutations in it are neutral, that is, without phenotypic effect. I argue here that such neutral change -and thus robustness -can be a key to future evolutionary innovation, if one accepts that neutrality is not an essential feature of a mutation. That is, a once neutral mutation may cause phenotypic effects in a changed environment or genetic background. I argue that most, if not all, neutral mutations are of this sort, and that the essentialist notion of neutrality should be abandoned. This perspective reconciles two opposing views on the forces dominating organismal evolution, natural selection and random drift: neutral mutations occur and are especially abundant in robust systems, but they do not remain neutral indefinitely, and eventually become visible to natural selection, where some of them lead to evolutionary innovations.

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Regulation of the Escherichia coli uncH gene by mRNA secondary structure and translational coupling

Cited by 15 publications

References 30 publications

Subunit δ Is the Key Player for Assembly of the H+-translocating Unit of Escherichia coli FOF1 ATP Synthase

Subunit δ Is the Key Player for Assembly of the H+-translocating Unit of Escherichia coli FOF1 ATP Synthase

Characterization of a b2δ Complex fromEscherichia coli ATP Synthase

Robustness, evolvability, and neutrality

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