A Selected Ribozyme Catalyzing Diverse Dipeptide Synthesis

Sun, Lele; Cui, Zhiyong; Gottlieb, Robert L; Zhang, Biliang

doi:10.1016/s1074-5521(02)00141-2

Cited by 45 publications

(27 citation statements)

References 23 publications

(7 reference statements)

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“…Other selected peptide bond-forming ribozymes also utilize adeylate as an acyl source. First, a peptide bond-forming ribozyme was selected that supposedly utilized an aminoacyl linked to the 3'-OH group of AMP [28], but the real substrate was later identified as a contaminating aminoacyl adenylate [29] (Fig. 3, a).…”

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confidence: 99%

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Ribozyme Catalysis of Metabolism in the RNA World

Chen¹,

Li²,

Ellington³

2007

Chemistry & Biodiversity

168

104

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In vitro selection has proven to be a useful means of explore the molecules and catalysts that may have existed in a primordial 'RNA world'. By selecting binding species (aptamers) and catalysts (ribozymes) from random sequence pools, the relationship between biopolymer complexity and function can be better understood, and potential evolutionary transitions between functional molecules can be charted. In this review, we have focused on several critical events or transitions in the putative RNA world: RNA self-replication; the synthesis and utilization of nucleotide-based cofactors; acyl-transfer reactions leading to peptide and protein synthesis; and the basic metabolic pathways that are found in modern living systems.

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confidence: 99%

“…3, b). Following up on these results, Zhang and co-workers intentionally selected ribozymes that could act as general dipeptide-synthesis catalysts by using aminoacyl adenylates as substrates [29].…”

mentioning

confidence: 99%

Ribozyme Catalysis of Metabolism in the RNA World

Chen¹,

Li²,

Ellington³

2007

Chemistry & Biodiversity

168

104

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“…49 other RNAs isolated by in vitro selection allow peptide bond formation in the absence of proteins including short RNA sequences. [102][103][104] Similarly, RNAs have been isolated that bind to amino acids with some specificity, primarily to amino acids with complex side chains. 105 61,107,108 Binding of amino acids and activated amino acids to sites created by small folded RNA molecules is clearly established and close proximity of such sites is entirely reasonable, but when it comes to the transition to ribosomal protein synthesis these hypotheses become vague.…”

Section: Coupled Nucleic Acid and Protein Synthesismentioning

confidence: 99%

An alternative to the RNA World Hypothesis

Francis

2011

Trends Evol Biol

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The RNA world hypothesis for the origin of life is widely accepted in spite of the complexity of RNA synthesis. An alternative hypothesis is advanced for the origin and evolution of protein and nucleic acid synthesis. From an early stage synthesis of the evolutionary predecessors of nucleic acids and polypeptides was coupled. This evolved into an RNA replication process that used 3'-aminoacyl-NMP monomers (N= pyrimidine or purine) with a singlet coding system in which the four bases coded for glycine, alanine, valine and aspartic acid. Ribosomal protein synthesis (RPS) evolved from coupled replication by using tRNAs and separating fidelity checking and peptide bond formation functions into small and large ribosomal subunits. Continuity was maintained during the transition to the triplet process by using the same catalysts that aminoacylated NMPs to aminoacylate four different bases at the 3' ends of the original tRNAs. Four GNC codons used the central base to designate the same four amino acids that were coded in singlet replication. Triplet-coded protein synthesis had the advantage of producing multiple copies of protein from a single copy of RNA, and eventually replaced protein synthesis via singlet-coded replication. Evolution of the simple triplet-coded process into RPS is described.

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“…An alternative synthetic mechanism that cannot be ruled out might be the direct incorporation of an Ala-Gly dipeptide into SacA. In this case, the dipeptide could originate from a highly active peptidyl transferase ribozyme (Sun et al ., 2002) or from proteolysis (H. von Döhren, pers. comm.…”

Section: Analysis Of the Sacabc Genes: The Nrps Systemmentioning

confidence: 99%

Molecular characterization of the safracin biosynthetic pathway from Pseudomonas fluorescens A2‐2: designing new cytotoxic compounds

Velasco

Acebo

Gómez

et al. 2005

Molecular Microbiology

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SummarySafracin is an antibiotic with anti-tumour activity produced by Pseudomonas fluorescens A2-2. The entire safracin synthetic gene cluster spanning 17.5 kb has been identified, cloned and sequenced. The safracin cluster comprises 10 open reading frames (ORFs) encoding proteins for three non-ribosomal peptide synthetases (NRPS), three safracin precursor biosynthetic enzymes, two safracin tailoring enzymes, a safracin resistance protein and a small hypothetical protein of unknown function. These genes are organized in two divergent operons of eight and two genes respectively. This pathway exhibits unusual features when compared with other NRPS systems. We have demonstrated by heterologous expression of the cluster that it is able to direct the synthesis of safracin in other strains. Cross-feeding experiments have confirmed that 3-hydroxy-5-methyl-O -methyltyrosine is the precursor of two amino acids of the molecule. Genetic analyses have allowed us to demonstrate that the bicistronic operon encodes the hydroxylation and N-methylation activities of the pathway. The cloning and expression of the safracin cluster has settled the basis for the in vivo and in vitro production of a wide variety of compounds, such as the promising ecteinascidins anti-cancer compounds.

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A Selected Ribozyme Catalyzing Diverse Dipeptide Synthesis

Cited by 45 publications

References 23 publications

Ribozyme Catalysis of Metabolism in the RNA World

Ribozyme Catalysis of Metabolism in the RNA World

An alternative to the RNA World Hypothesis

Molecular characterization of the safracin biosynthetic pathway from Pseudomonas fluorescens A2‐2: designing new cytotoxic compounds

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