Oligoribonucleotide synthesis. X. An improved synthesis of the anticodon loop region of methionine transfer ribonucleic acid from E. coli

1976 ◽  
Vol 54 (17) ◽  
pp. 2689-2696 ◽  
Author(s):  
E. S. Werstiuk ◽  
Thomas Neilson
Keyword(s):  
Ribonucleic Acid ◽  
Coupling Efficiency ◽  
Transfer Rna ◽  
Its Sequence ◽  
Anticodon Loop ◽  
E Coli ◽  
Loop Region ◽  
Phosphotriester Method

Nonaribonucleotide, GpCmpUpCpApUpApApC, was synthesized using a block phosphotriester method. Its sequence corresponds to that of the anticodon loop of transfer RNAfMet (E. coli). Protected tetramer, GCmUC and pentamer nucleotides, AUAAC, assembled stepwise from nucleoside derivatives, were joined together to give protected nonamer which on deblocking, gave the free nonaribonucleotide in milligram amounts. The superior internucleotide coupling efficiency of mesitylenesulfonyl triazolide (MST) over triisopropylbenzenesulfonyl chloride (TPS) is demonstrated.

scholarly journals The effect of hypermethylation on the functional properties of transfer ribonucleic acid. Formation of aminoacyl-transfer-ribonucleic acid

1969 ◽  
Vol 114 (2) ◽  
pp. 429-435 ◽  
Author(s):  
David J. Pillinger ◽  
John Hay ◽  
Ernest Borek
Keyword(s):  
Amino Acids ◽  
Ribonucleic Acid ◽  
Control Sample ◽  
Transfer Rna ◽  
E Coli ◽  
Functional Sites ◽  
The Individual ◽  
Almost All ◽  
Aminoacyl Transfer ◽  
Kinetics Of

1. The ability of chemically hypermethylated Escherichia coli B transfer RNA to accept 19 amino acids was studied and the results were compared with those obtained with a control sample of E. coli B transfer RNA incubated under similar conditions in the absence of methylating agent. 2. There is a marked decrease in the ability of the modified transfer RNA to accept amino acids in almost all instances. 3. The acceptance of cysteine appears to be unique in that it is enhanced in the hypermethylated transfer RNA. 4. More detailed studies on the kinetics of acceptance for six amino acids is presented, emphasizing the variation in response of the individual amino acids. 5. Increasing hypermethylation causes a progressive decrease in the amino acid acceptance. 6. The results are discussed in terms of methylation at functional sites within the transfer RNA and possible conformational alterations to the structure of the macromolecule.

Interaction specificity between the chaperone and proteolytic components of the cyanobacterial Clp protease

2012 ◽  
Vol 446 (2) ◽  
pp. 311-320 ◽  
Author(s):  
Anders Tryggvesson ◽  
Frida M. Ståhlberg ◽  
Axel Mogk ◽  
Kornelius Zeth ◽  
Adrian K. Clarke
Keyword(s):  
Escherichia Coli ◽  
Active Sites ◽  
Terminal Sequence ◽  
Core Complex ◽  
Clp Protease ◽  
E Coli ◽  
Loop Region ◽  
N Terminus ◽  
Specific Association ◽  
The Stability

The Clp protease is conserved among eubacteria and most eukaryotes, and uses ATP to drive protein substrate unfolding and translocation into a chamber of sequestered proteolytic active sites. In plant chloroplasts and cyanobacteria, the essential constitutive Clp protease consists of the Hsp100/ClpC chaperone partnering a proteolytic core of catalytic ClpP and noncatalytic ClpR subunits. In the present study, we have examined putative determinants conferring the highly specific association between ClpC and the ClpP3/R core from the model cyanobacterium Synechococcus elongatus. Two conserved sequences in the N-terminus of ClpR (tyrosine and proline motifs) and one in the N-terminus of ClpP3 (MPIG motif) were identified as being crucial for the ClpC–ClpP3/R association. These N-terminal domains also influence the stability of the ClpP3/R core complex itself. A unique C-terminal sequence was also found in plant and cyanobacterial ClpC orthologues just downstream of the P-loop region previously shown in Escherichia coli to be important for Hsp100 association to ClpP. This R motif in Synechococcus ClpC confers specificity for the ClpP3/R core and prevents association with E. coli ClpP; its removal from ClpC reverses this core specificity.

ORGANISATION AND EXPRESSION OF THE E. COLI PHENYLALANYL-TRANSFER RNA SYNTHETASE OPERON

1982 ◽  
pp. 25-47 ◽  
Author(s):  
MATHIAS SPRINGER ◽  
JACQUELINE PLUMBRIDGE ◽  
MARIE TRUDEL ◽  
MARIANNE GRUNBERG-MANAGO ◽  
GUY FAYAT ◽  
...  
Keyword(s):  
Transfer Rna ◽  
E Coli

Oligoribonucleotide synthesis. IX. Synthesis of sequences corresponding to the dihydrouridine loop neck region common in several transfer RNA molecules

1976 ◽  
Vol 54 (11) ◽  
pp. 1714-1721 ◽  
Author(s):  
T. E. England ◽  
Thomas Neilson
Keyword(s):  
Neck Region ◽  
Transfer Rna ◽  
Coupling Reactions ◽  
Special Significance ◽  
Transfer Rnas ◽  
Rna Molecules ◽  
Activating Agent ◽  
Phosphotriester Method

The syntheses of the oligoribonucleotides GpApGpC, GpCpUpC, and ApGpCpUpC by an improved phosphotriester method are described. These sequences are found in the double-stranded region adjacent to the dihydrouridine loop of several transfer RNAs. Of special significance is the improvement in yields that the activating agent, mesitylenesulfonyl triazolide, provides in coupling reactions involving purine residues.

Transfer RNA Identity Change in Anticodon Variants of E. coli tRNAPhe in Vivo

2000 ◽  
Vol 10 (1) ◽  
pp. 76-82 ◽  
Author(s):  
Hyun-Soo Kim ◽  
Ick Young Kim ◽  
Dieter Söll ◽  
Se Yong Lee
Keyword(s):  
Transfer Rna ◽  
Identity Change ◽  
E Coli
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