Same Same but Different: New Structural Insight into CRISPR-Cas Complexes

Three papers in this issue of Molecular Cell report on the structure and functional activity of type III CRISPR-Cas effector complexes, revealing novel and conserved features of the ribonucleoprotein particles that underlie prokaryotic genome defense. The new structures suggest that type I and type...

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Veröffentlicht in:	Molecular cell 2013-10, Vol.52 (1), p.4-7
Hauptverfasser:	Heidrich, Nadja, Vogel, Jörg
Format:	Artikel
Sprache:	eng
Schlagworte:	amino acid sequences Archaeal Proteins - chemistry Archaeal Proteins - metabolism Bacterial Proteins - metabolism complexing CRISPR-Associated Proteins - chemistry CRISPR-Associated Proteins - metabolism genome genomes Pyrococcus furiosus - metabolism Ribonucleases - metabolism ribonucleoproteins RNA RNA Interference RNA, Archaeal - metabolism RNA, Bacterial - metabolism structures Sulfolobus solfataricus - metabolism Thermus thermophilus - metabolism
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Beschreibung
Zusammenfassung:	Three papers in this issue of Molecular Cell report on the structure and functional activity of type III CRISPR-Cas effector complexes, revealing novel and conserved features of the ribonucleoprotein particles that underlie prokaryotic genome defense. The new structures suggest that type I and type III complexes follow the same architectural principles and are most likely descendants of a common ancestor, the differences in RNA and protein sequences and structure of individual components notwithstanding.
ISSN:	1097-2765 1097-4164
DOI:	10.1016/j.molcel.2013.09.023