Abstract:
BACKGROUND: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. RESULTS: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. CONCLUSION: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). REVIEWERS:This article was reviewed by Sergey Melnikov and Igor Rogozin. OPEN PEER REVIEW:Reviewed by Sergey Melnikov and Igor Rogozin. For the full reviews, please go to the Reviewers' comments section.
journal_name
Biol Directjournal_title
Biology directauthors
Lisitsyna OM,Kurnaeva MA,Arifulin EA,Shubina MY,Musinova YR,Mironov AA,Sheval EVdoi
10.1186/s13062-020-00263-6subject
Has Abstractpub_date
2020-04-28 00:00:00pages
9issue
1issn
1745-6150pii
10.1186/s13062-020-00263-6journal_volume
15pub_type
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