<i>Helicobacter pylori </i><scp>HP</scp>0425 Targets the Nucleus with <scp>DN</scp>ase I‐Like Activity

Kim, Jung-Min; Choe, Min-Ho; Asaithambi, Killivalavan; Song, Jae‐Young; Lee, Yong Seok; Lee, Je Chul; Seo, Ji‐Hyun; Kang, Hyung-Lyun; Lee, Kon Ho; Cho, Myung-Je; Rhee, Kwang‐Ho; Youn, Hee‐Shang; Baik, Seung‐Chul

doi:10.1111/hel.12271

Cited by 8 publications

(8 citation statements)

References 31 publications

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“…1f; Supplementary Table S2). These data are in agreement with published results indicating that NLSs are present not only in the proteins of eukaryotes but also in the proteins of prokaryotes [15][16][17][18][19][20][21][22] and bacteriophages [23].…”

Section: Resultssupporting

confidence: 93%

“…We substantially modified the sentence "We propose that the pre-existence of NLSs inside prokaryotic proteins dictated, at least partially, the nuclear proteome composition". Our logic was based on the data presented as well as on some published results (references [15][16][17][18][19][20][21][22][23]), which indicate that the NLSs in modern eukaryotic proteins might have evolved from the DNA-binding domains of prokaryotic proteins. As a result, some DNAbinding domains are sufficient for interaction with karyopherins, and as a consequence, a protein may have had features of a nuclear protein before the origin of the cell nucleus.…”

Section: Reviewer Commentsmentioning

confidence: 99%

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

et al. 2020

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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.

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Section: Resultssupporting

confidence: 93%

Section: Reviewer Commentsmentioning

confidence: 99%

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

et al. 2020

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“…These data are in agreement with published results indicating that NLSs are present not only in the proteins of eukaryotes but also in the proteins of prokaryotes [15][16][17][18][19][20][21][22] and bacteriophages [23].…”

Section: Resultssupporting

confidence: 93%

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

Lisitsyna

Kurnaeva

Arifulin

et al. 2020

Preprint

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AbstractThe 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, was one of the most important events in the evolution of the eukaryotic cell. How the proteins were selected for import into the forming nuclei remains an open question. Here, we demonstrate that functional NLSs may be integrated inside nucleotide-binding domains of both eukaryotic and prokaryotic proteins and may co-evolve with these domains. We propose that the pre-existence of NLSs inside prokaryotic proteins dictated, at least partially, the nuclear proteome composition.

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“…To enter the nucleus, proteins use short signal sequences, known as nuclear localization signals (NLSs) (Lange et al 2007;Paci et al 2021). Sequences similar or identical to eukaryotic NLSs are present in proteins in different prokaryotes (Rossi et al 1993;Nederlof et al 1995;Perić et al 2008;Lee et al 2012;Moon et al 2012;Kim et al 2016;Kwon et al 2016;Lisitsyna et al 2020;Melnikov et al 2020), indicating that the origin of NLSs precedes the separation of the nucleus and the cytoplasm. This integration of NLS(s) into different (mostly DNA-and/or RNA-binding) domains was also observed in modern Eukaryota (LaCasse and Lefebvre 1995; Cokol et al 2000;Melnikov et al 2015;Kharitonov et al 2020;Lisitsyna et al 2020).…”

Section: Introductionmentioning

confidence: 99%

“…To enter the nucleus, proteins use short signal sequences, known as nuclear localization signals (NLSs) (2,3). Sequences similar or identical to eukaryotic NLSs are present in proteins in different prokaryotes (4)(5)(6)(7)(8)(9)(10)(11)(12), indicating that the origin of NLSs precedes the separation of the nucleus and the cytoplasm. This integration of NLS(s) into different (mostly DNA-and/or RNA-binding) domains was also observed in modern Eukaryota (11,(13)(14)(15)(16).…”

mentioning

confidence: 99%

Molecular coevolution of nuclear and nucleolar localization signals inside basic domain of HIV-1 Tat

Kurnaeva¹,

Zalevsky

Arifulin³

et al. 2021

Preprint

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During evolution, viruses had to adapt to an increasingly complex environment of eukaryotic cells. Viral proteins that need to enter the cell nucleus or associate with nucleoli possess nuclear localization signals (NLSs) and nucleolar localization signals (NoLSs) for nuclear and nucleolar accumulation, respectively. As viral proteins are relatively small, acquisition of novel sequences seems to be a more complicated task for viruses than for eukaryotes. Here, we carried out a comprehensive analysis of the basic domain (BD) of HIV-1 Tat to show how viral proteins might evolve with NLSs and NoLSs without an increase in protein size. The HIV-1 Tat BD is involved in several functions, the most important being the transactivation of viral transcription. The BD also functions as an NLS, although it is substantially longer than a typical NLS. It seems that different regions in the BD could function as NLSs due to its enrichment with positively charged amino acids. Additionally, the high positive net charge inevitably causes the BD to function as an NoLS through a charge-specific mechanism. The integration of NLSs and NoLSs into functional domains enriched with positively charged amino acids might be a mechanism that allows the condensation of different functional sequences in small protein regions and, as a result, to reduce protein size, influencing the origin and evolution of NLSs and NoLSs in viruses.

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Helicobacter pylori HP0425 Targets the Nucleus with DNase I‐Like Activity

Abstract: These results suggest that HP0425 carrying a nuclear localization signal sequence translocates into the nucleus of host cells and degrades genomic DNA by DNase I-like enzymatic activity, which is a new pathogenic strategy of H. pylori in the host.

Cited by 8 publications

References 31 publications

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

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

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

Molecular coevolution of nuclear and nucleolar localization signals inside basic domain of HIV-1 Tat

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