Origin of the nuclear proteome on the basis of pre-existing nuclear localization signals in prokaryotic proteins

• Published in: Biology direct Vol. 15; no. 1; p. 9
• Main Authors: Lisitsyna, Olga M, Kurnaeva, Margarita A, Arifulin, Eugene A, Shubina, Maria Y, Musinova, Yana R, Mironov, Andrey A, Sheval, Eugene V
• Format: Journal Article
• Language: English
• Published: England BioMed Central Ltd 28-04-2020; BioMed Central; BMC
• Subjects: Amino acids; Annotations; Binding; Cloning; Deoxyribonucleic acid; DNA; Evolution; Gene expression; Gene sequencing; Imports; Localization; Mutagenesis; Nuclear localization signal; Nuclear proteome; Nuclei (cytology); Nucleotide sequence; Nucleotides; Nucleus; Pelodiscus sinensis; Protein binding; Protein transport; Proteins; Proteomes; Nuclear localization signal; Nuclear proteome; Nucleus; Evolution
• ISSN: 1745-6150; 1745-6150
• DOI: 10.1186/s13062-020-00263-6

The origin of the selective nuclear protein import machinery, which consists of nuclear pore complexes and adaptor molecules interacting with the nuclear localization signals (NLSs) of cargo molecules, is one of the most important events in the evolution of eukaryotic cells. How proteins were selected for import into the forming nucleus remains an open question.
Here, we demonstrate that functional NLSs may be integrated in the nucleotide-binding domains of both eukaryotic and prokaryotic proteins and may coevolve with these domains.
The presence of sequences similar to NLSs in the DNA-binding domains of prokaryotic proteins might have created an advantage for nuclear accumulation of these proteins during evolution of the nuclear-cytoplasmic barrier, influencing which proteins accumulated and became compartmentalized inside the forming nucleus (i.e., the content of the nuclear proteome).
This article was reviewed by Sergey Melnikov and Igor Rogozin.
Reviewed by Sergey Melnikov and Igor Rogozin. For the full reviews, please go to the Reviewers' comments section.