Role of leader peptide synthesis in repZ gene expression of the ColIb-P9 plasmid.

Hama, Chihiro; Takizawa, Takenori; Moriwaki, H; Mizobuchi, Kiyoshi

doi:10.1016/s0021-9258(18)86998-8

Cited by 31 publications

(3 citation statements)

References 35 publications

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“…Several other plasmids use the same mechanism of control. A subfamily of plasmids 12,23 (belonging to incompatibility groups IncIa, IncB, and others) displays an additional layer of complexity: once the leader peptide has been translated, a long-distance RNA pseudoknot is formed that keeps the rep RBS stem-loop open and translationally active.…”

Section: Entry From Upstream: Breaking Structure and Translational Couplingmentioning

confidence: 99%

“…Structures in 5'-leaders of mRNAs (often encompassing the RBS), are also frequently sites at which post-transcriptional control is exerted. This may occur by binding of regulatory proteins-as is the case for control of most ribosomal protein genes 9 and threonine aminoacyl-tRNA synthetase (thrS), 10 or regulatory noncoding antisense RNAs-as in control of plasmid replication initiator proteins 11,12 and many bacterial stress-related genes. 13 Furthermore, structure and sequence accessibility can also be controlled by metabolites (through riboswitches 14 ) or temperature.…”

Section: Introductionmentioning

confidence: 99%

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Dealing with stable structures at ribosome binding sites: Bacterial translation and ribosome standby

Unoson¹,

Wagner²

2007

RNA Biology

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Bacterial ribosomes have great difficulties to initiate translation on stable structures within mRNAs. Translational coupling and induced structure changes are strategies to open up inhibitory RNA structures encompassing ribosome binding sites (RBS). There are, however, mRNAs in which stable structures are not unfolded, but that are nevertheless efficiently initiated at high rates. de Smit and van Duin(1) proposed a "ribosome standby" model to theoretically solve this paradox: the 30S ribosome binds nonspecifically to an accessible site on the mRNA (standby site), waiting for a transient opening of a stable RBS hairpin. Upon unfolding, the 30S subunit relocates to form a productive initiation complex. Recent reports have provided experimental support for this model. This review will describe and compare two different flavors of standby sites, their properties, and their likely implications. We also discuss the possibility that ribosome standby may be a more general strategy to obtain high translation rates.

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Section: Entry From Upstream: Breaking Structure and Translational Couplingmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Dealing with stable structures at ribosome binding sites: Bacterial translation and ribosome standby

Unoson¹,

Wagner²

2007

RNA Biology

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“…Genetic analysis of this system identified compensatory base changes between short complementary sequences 107 bases apart, one upstream of repY and one within the repY coding region (Asano et al, 1991). The upstream sequence is within the hairpin loop of a predicted very stable hairpin (Hama et al, 1990) and thus potentially forms a pseudoknot; the downstream sequence is just 5' to the repZ Shine-Dalgarno sequence and could alternatively form a stable hairpin with the repZ ribosome binding site. Asano et al (1991) propose that translation of repY disrupts the repZ ribosome binding site hairpin, and that the pseudoknot then forms as an alternative structure which unmasks the repZ initiation site and stimulates its translation.…”

Section: Messenger Rnasmentioning

confidence: 99%

Structural and functional aspects of RNA pseudoknots

Dam¹,

Pleij²,

Draper³

1992

Biochemistry

169

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Replication control of plasmid R1: RepA synthesis is regulated by CopA RNA through inhibition of leader peptide translation.

1992

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The replication frequency of plasmid R1 is post‐transcriptionally controlled by an antisense RNA, CopA, that binds to the leader region in the RepA mRNA, CopT, and ultimately inhibits the synthesis of the replication initiator protein RepA. We present results demonstrating that CopA controls RepA synthesis indirectly. A reading frame for a 24 amino acid leader peptide (Tap, translational activator peptide) is located in the region between the copA and repA genes. A translational fusion between the tap and lacZ genes was used to demonstrate that tap is translated and controlled by CopA. Stop codons (UAA, UAG and UGA) introduced at three different positions within the tap gene led to a severe decrease in repA expression. Specific suppression of the stop codons reversed the effect. This indicates that tap translation is required for RepA synthesis. Phylogenetic comparisons between IncFII‐like plasmids, together with previous in vitro and in vivo results (Ohman and Wagner, 1989, 1991), suggest that a stable RNA stem‐loop structure sequesters the repA ribosome binding site irrespective of CopA‐CopT duplex formation. The results presented here show that ribosomes translating the tap reading frame have to terminate close to the start codon of repA to permit reinitiation (direct translational coupling), and that transient disruption of the inhibitory RNA stem‐loop is insufficient for activation of repA translation. The possibility that direct translational coupling is required because of a suboptimal repA RBS cannot be excluded.(ABSTRACT TRUNCATED AT 250 WORDS)

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Role of leader peptide synthesis in repZ gene expression of the ColIb-P9 plasmid.

Cited by 31 publications

References 35 publications

Dealing with stable structures at ribosome binding sites: Bacterial translation and ribosome standby

Dealing with stable structures at ribosome binding sites: Bacterial translation and ribosome standby

Structural and functional aspects of RNA pseudoknots

Replication control of plasmid R1: RepA synthesis is regulated by CopA RNA through inhibition of leader peptide translation.

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