Protein P tetramer binds protein L

Stable Identifier
R-HSA-9830236
Type
Reaction [binding]
Species
Homo sapiens
Related Species
Human respiratory syncytial virus A
Compartment
cytosol
ReviewStatus
5/5
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Protein P tetramer binds protein L
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Protein P tetramer forms a complex with protein L, the RNA-dependent RNA polymerase of the respiratory syncytial virus (RSV). In this complex, every protein P monomer takes a distinct conformation (Gilman et al. 2019), which is likely governed by intrinsically disordered N- and C-terminal regions of the P protein (Cardone et al. 2021). Disordered regions of the P protein are compatible with weak interactions required for the processivity of the polymerase complex (Pereira et al. 2017). The complex of protein L with protein P is catalytically active, but exhibits a low processivity (Gilman et al. 2019). Besides its RNA-dependent RNA polymerase (RdRp) domain, protein L possesses two other enzymatic domains: the polyribonucleotidyltransferase (PRNTase or capping) domain, and the methyltransferase (MTase) domain. The MTase domain catalyzes cap methylation (reviewed by Fearns 2019). The RdRP and capping domains of L interact with the oligomerization domain and the C-terminal domain of the P tetramer (Cao et al. 2020). Hydrophobic residues in the C-terminus of P protein, upstream of the C-terminal N protein binding site, are involved in binding to the L protein (Sourimant et al. 2015).
Literature References
PubMed ID Title Journal Year
25653447 Fine mapping and characterization of the L-polymerase-binding domain of the respiratory syncytial virus phosphoprotein

Sourimant, J, Rameix-Welti, MA, Gaillard, AL, Chevret, D, Galloux, M, Gault, E, Eléouët, JF

J Virol 2015
31953395 Cryo-EM structure of the respiratory syncytial virus RNA polymerase

Cao, D, Gao, Y, Roesler, C, Rice, S, D'Cunha, P, Zhuang, L, Slack, J, Domke, M, Antonova, A, Romanelli, S, Keating, S, Forero, G, Juneja, P, Liang, B

Nat Commun 2020
31495574 Structure of the Respiratory Syncytial Virus Polymerase Complex

Gilman, MSA, Liu, C, Fung, A, Behera, I, Jordan, P, Rigaux, P, Ysebaert, N, Tcherniuk, S, Sourimant, J, Eléouët, JF, Sutto-Ortiz, P, Decroly, E, Roymans, D, Jin, Z, McLellan, JS

Cell 2019
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Cross References
Mondo
Authored
Orlic-Milacic, M  (2023-02-28)
Reviewed
Bergeron, HC  (2023-11-03)
Created
Orlic-Milacic, M  (2023-02-28)
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