Authors:
Nosalskaya, Tatiana Nikolaevna,, Martynov, Artur Viktorovich,, Bomko, Tatiana Vasilievna
Abstract:
The review provides data about nuclear localization signal peptides (NLS) and their function in the cell, incl. with a viral infection process. The binding, penetration, assembly, and budding of viruses are currently being intensively studied in many systems. However, the stages of nuclear transport during the penetration and release of the virus have remained practically unexplored. NLS were first identified in the large T antigen virus SV40 and from nucleoplasmin, and then were identified in a large number of proteins. They usually contain sh (...)
The review provides data about nuclear localization signal peptides (NLS) and their function in the cell, incl. with a viral infection process. The binding, penetration, assembly, and budding of viruses are currently being intensively studied in many systems. However, the stages of nuclear transport during the penetration and release of the virus have remained practically unexplored. NLS were first identified in the large T antigen virus SV40 and from nucleoplasmin, and then were identified in a large number of proteins. They usually contain short base peptides includes lysine or arginine residues in the form of mono- or bipartite signals. NLSs include the "pat4" motif, which consists of a contiguous stretch four essential amino acids (arginine and lysine). Both coronaviruses and arteriviruses show similar genomic organization and belong to Nidovirales. Although both families encode nucleoproteins (N-proteins), the main function of which is to bind viral RNA, NLS-containing proteins has different sizes and do not have significant homology. The review provides the characteristics and structure of NLS for many viral proteins, and shows their role in the pathogenicity of viruses.
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