RNase III-dependent hydrolysis of lambda cII-O gene mRNA mediated by lambda OOP antisense RNA.

Krinke, Lothar; Wulff, Daniel L.

doi:10.1101/gad.4.12a.2223

Cited by 82 publications

(68 citation statements)

References 14 publications

(20 reference statements)

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“…5 A-C) (23) and coincides with the region encoding the CII protease-sensitive target. OOP acts as an antisense RNA to CII and reduces CII expression by increasing the rate of CII mRNA hydrolysis, which is initiated by cleavage of the double-stranded RNA by RNase III (24). On cells, in which OOP RNA is expressed, in trans from a plasmid, WT and cII DD form clear plaques, whereas cII 1-81 and cII form turbid plaques.…”

Section: (ᮀ) (D)mentioning

confidence: 99%

The phage λ CII transcriptional activator carries a C-terminal domain signaling for rapid proteolysis

Kobiler

Koby

Teff

et al. 2002

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

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ATP-dependent proteases, like FtsH (HflB), recognize specific protein substrates. One of these is the CII protein, which plays a key role in the phage lysis-lysogeny decision. Here we provide evidence that the conserved C-terminal end of CII acts as a necessary and sufficient cis-acting target for rapid proteolysis. Deletions of this conserved tag, or a mutation that confers two aspartic residues at its C terminus do not affect the structure or activity of CII. However, the mutations abrogate CII degradation by FtsH. We have established an in vitro assay for the CIII protein and demonstrated that CIII directly inhibits proteolysis by FtsH to protect CII and CII mutants from degradation. Phage carrying mutations in the C terminus of CII show increased frequency of lysogenization, which indicates that this segment of CII may itself be sensitive to regulation that affects the lysis-lysogeny development. In addition, the region coding for the C-terminal end of CII overlaps with a gene that encodes a small antisense RNA called OOP. We show that deletion of the end of the cII gene can prevent OOP RNA, supplied in trans, interfering with CII activity. These findings provide an example of a gene that carries a region that modulates stability at the level of mRNA and protein. Proteolysis by ATP-dependent proteases is an important mechanism for the rapid control of gene activity, the removal of unfolded inactive proteins, and the elimination of incomplete polypeptides. In bacteria, proteolysis acts on key regulatory transcription factors affecting the heat shock ( 32 ), stationary phase ( s ), and the SOS DNA repair system (LexA) responses, capsular polysaccharide biosynthesis, and the control of the lysis-lysogeny decision of phage (1). FtsH is a membranebound ATP-dependent protease in which the ATPase domain and the protease domain are linked in one polypeptide (2). FtsH orthologs are found within mitochondria and chloroplasts in higher organisms (3, 4). The number of native proteins known to be substrates for FtsH is rather small and includes the heat shock sigma factor 32 , SecY, YccA, subunit a of the membraneembedded F 0 part of the H ϩ -ATPase, as well as phage CII, CIII, and Xis proteins (see ref. 5). However, the signal(s) by which these native substrates are recognized by FtsH is not known. FtsH, as well as Tsp, ClpAP, and ClpXP recognize the SsrA peptide tag that is added to the C terminus of incomplete proteins by trans-translation (6).The lysogenic response established after infection of Escherichia coli by the temperate bacteriophage requires the initial synthesis of the CI repressor from the pE promoter and the integration protein Int, from the pI promoter. In addition, establishment of viable lysogenic cells requires the expression of the paQ promoter that inhibits lytic gene expression. The phage CII protein, which is 97 amino acid residues long, plays a key initiating role in these processes by activating the pE, pI, and paQ promoters (7). CII itself is regulated at many levels: transcription, translatio...

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Section: (ᮀ) (D)mentioning

confidence: 99%

The phage λ CII transcriptional activator carries a C-terminal domain signaling for rapid proteolysis

Kobiler

Koby

Teff

et al. 2002

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

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“…In the E. coli R1-encoded hok/sok system and the E. faecalis pAD1-encoded par system, the antitoxin is a relatively unstable regulatory RNA that binds to the toxin mRNA and prevents translation. Addiction systems present special problems for antisense RNA regulation since the rapid degradation of the RNA-RNA complexes that occur in most negatively regulated systems (2,5,12,22) would leave no toxin message to be translated once the plasmid is lost. In the hok/sok system (10), this problem is solved by the accumulation of a pool of a conformation of the hok mRNA that neither binds the Sok antisense regulator nor allows ribosome binding (29).…”

mentioning

confidence: 99%

Translational Regulation by an Intramolecular Stem-Loop Is Required for Intermolecular RNA Regulation of theparAddiction Module

et al. 2008

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The par stability determinant of Enterococcus faecalis plasmid pAD1 is the only antisense RNA-regulated addiction module identified to date in gram-positive bacteria. par encodes two small, convergently transcribed RNAs, designated RNA I and RNA II, that function as the toxin (Fst)-encoding and antitoxin components, respectively. Previous work showed that structures at the 5 end of RNA I are important in regulating its translation. The work presented here reveals that a stem-loop sequestering the Fst ribosome binding site is required for translational repression but a helix sequestering the 5 end of RNA I is not. Furthermore, disruption of the stem-loop prevented RNA II-mediated repression of Fst translation in vivo. Finally, although Fst-encoding wild-type RNA I is not toxic in Escherichia coli, mutations affecting stem-loop stability resulted in toxicity in this host, presumably due to increased translation.

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“…The promoter direction is inverted in orientation to these genes. In the λ phage, the RNA regulated by the corresponding promoter is thought to be an antisense RNA (Krinke and Wulff, 1990), which hybridizes the 5 -untranslated region of the mRNA for CII and the level of translation from the mRNA is reduced. In the λ phage, the CII protein is the activator of CI protein which plays an important role for the maintenance of lysogeny and prophage induction.…”

Section: Determination Of Lexa Binding Sequences In Newly Identifi Edmentioning

confidence: 99%

Identification of LexA regulated promoters in Escherichia coli O157:H7

Yaguchi

Mikami

Igari

et al. 2011

J. Gen. Appl. Microbiol.

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In Escherichia coli (E. coli), most DNA damage-inducible (din) genes belong to the LexA regulon, whose products are related to functions such as DNA repair and induced mutagenesis. The E. coli K-12 cells have about 30 operons that are known to be members of the LexA regulon. LexA acts as a transcriptional repressor of these unlinked genes by binding to the specifi c DNA sequences located within the promoter regions. We developed a genetic screening method to isolate LexA dependent promoters. By using an applied whole-genome shotgun method with a lac-operon system, we isolated promoter candidates of din genes from the E. coli O157:H7 genome. We found that transcriptional repression from most of these promoters was dependent on lexA and purifi ed LexA protein bound directly to the DNA fragments carrying them. Finally, we identifi ed 16 and 5 promoters that regulated expression of previously known and novel LexA dependent genes, respectively. In addition to them, we also identifi ed 2 antisense promoters which were considered to regulate expression of antisense RNAs for mRNAs of the ecs1779 and ecs2988 genes. All newly identifi ed promoter regions contained DNA sequences similar to the consensus LexA binding sequence.

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RNase III-dependent hydrolysis of lambda cII-O gene mRNA mediated by lambda OOP antisense RNA.

Cited by 82 publications

References 14 publications

The phage λ CII transcriptional activator carries a C-terminal domain signaling for rapid proteolysis

The phage λ CII transcriptional activator carries a C-terminal domain signaling for rapid proteolysis

Translational Regulation by an Intramolecular Stem-Loop Is Required for Intermolecular RNA Regulation of theparAddiction Module

Identification of LexA regulated promoters in Escherichia coli O157:H7

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