The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release

Article Abstract:

Peptide bond formation and peptide release are catalyzed in the active site of the ribosome, which is composed of two layers of conserved nucleotides. Results of a study on the use of an affinity-tagging system for the purification of mutant ribosomes and analysis of four universally conserved nucleotides in the innermost layer of the active site show a distinct inner shell that is pivotal for peptide release, and an outer shell responsible for peptide bond formation.

Nucleic Acid Derivatives, Composition, Ribosomes, Binding sites (Biochemistry), Active sites (Biochemistry), Nucleotides, Chemistry, Analytic, Analytical chemistry, Chemical properties

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Role for the PP2A/B56[delta] phosphatase in regulating 14-3-3 release from Cdc25 to control mitosis

Article Abstract:

The DNA-responsive checkpoints are found to activate PP2A/B56[delta] phosphatase complexes to dephosphorylate Cdc25 at a site distinct from Ser287 (T138), the phosphorylation of which is required for 14-3-3 release. The results have identified PP2A/B56[delta] as a vital checkpoint effector and have described a mechanism for showing that a critical component of checkpoint regulation lies with the PP2A-mediated dephosphorylation of T128 and consequent release of 14-3-3.

Phosphorylation, Phosphatases

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Transcriptional pausing caught in the act

Article Abstract:

Single-molecule techniques allow the tracking of a transcription complex, along a deoxyribonucleic acid (DNA) template in real time and to 1 bp resolution. A team of scientists exploits this approach to study a central component of transcription regulation, the sequence-dependent pausing of ribonucleic acid (RNA) polymerase during transcript elongation.

Genetic transcription, Transcription (Genetics), RNA polymerases

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