Structural disorder and modular organization in Paramyxovirinae N and P.
The existence and extent of disorder within the replicative complex (N, P and the polymerase, L) of Paramyxovirinae were investigated, drawing on the discovery that the N-terminal moiety of the phosphoprotein (P) and the C-terminal moiety of the nucleoprotein (N) of measles virus are intrinsically unstructured. We show that intrinsic disorder is a widespread property within Paramyxovirinae N and P, using a combination of different computational approaches relying on different physico-chemical concepts. Notably, experimental support that has often gone unnoticed for most of the predictions has been found in the literature. Identification of disordered regions allows the unveiling of a common organization in all Paramyxovirinae P, which are composed of six modules defined on the basis of structure or sequence conservation. The possible functional significance of intrinsic disorder is discussed in the light of experimental data, which show that unstructured regions of P and N are involved in numerous interactions with several protein and protein-RNA partners. This study provides a contribution to the rather poorly investigated field of intrinsically disordered proteins and helps in targeting protein domains for structural studies.
Karlin
David
D
Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS et Université Aix-Marseille I et II, ESIL, Campus de Luminy, 13288 Marseille Cedex 09, France.
Ferron
François
F
Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS et Université Aix-Marseille I et II, ESIL, Campus de Luminy, 13288 Marseille Cedex 09, France.
Canard
Bruno
B
Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS et Université Aix-Marseille I et II, ESIL, Campus de Luminy, 13288 Marseille Cedex 09, France.
Longhi
Sonia
S
Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS et Université Aix-Marseille I et II, ESIL, Campus de Luminy, 13288 Marseille Cedex 09, France.
D000595:Amino Acid Sequence; D004268:DNA-Binding Proteins; D029721:Drosophila Proteins; D008969:Molecular Sequence Data; D018103:Morbillivirus / Q000737:chemistry; D009419:Nerve Tissue Proteins; D009698:Nucleoproteins / Q000737:chemistry* / Q000235:genetics; D018098:Paramyxovirinae / Q000737:chemistry* / Q000235:genetics; D010750:Phosphoproteins / Q000737:chemistry*; D017433:Protein Structure, Secondary; D011518:Proto-Oncogene Proteins / Q000737:chemistry; D019213:Rubulavirus / Q000737:chemistry; D016415:Sequence Alignment; D014157:Transcription Factors; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics
D004268:DNA-Binding Proteins; D029721:Drosophila Proteins; D009419:Nerve Tissue Proteins; D009698:Nucleoproteins; D010750:Phosphoproteins; D011518:Proto-Oncogene Proteins; D014157:Transcription Factors; D014764:Viral Proteins; C083884:pnt protein, Drosophila