CRISPR-Associated Primase-Polymerases are implicated in
prokaryotic CRISPR-Cas adaptation

J 2021

CRISPR-Associated Primase-Polymerases are implicated in prokaryotic CRISPR-Cas adaptation

ZABRADY, Katerina, Matej ZABRADY, Peter KOLESÁR, Arthur W. H. LI, Aidan J. DOHERTY et. al.

Basic information

Original name

CRISPR-Associated Primase-Polymerases are implicated in prokaryotic CRISPR-Cas adaptation

Authors

ZABRADY, Katerina, Matej ZABRADY, Peter KOLESÁR (703 Slovakia, belonging to the institution), Arthur W. H. LI and Aidan J. DOHERTY

Edition

Nature Communications, London, Nature Publishing Group, 2021, 2041-1723

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10603 Genetics and heredity

Country of publisher

Germany

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 17.694

RIV identification code

RIV/00216224:14310/21:00123820

Organization unit

Faculty of Science

DOI

http://dx.doi.org/10.1038/s41467-021-23535-9

UT WoS

000665032700012

Keywords in English

CRISPR-Cas systems; DNA; DNA repair enzymes; Enzyme mechanisms

Abstract

V originále

CRISPR-Cas pathways provide prokaryotes with acquired "immunity" against foreign genetic elements, including phages and plasmids. Although many of the proteins associated with CRISPR-Cas mechanisms are characterized, some requisite enzymes remain elusive. Genetic studies have implicated host DNA polymerases in some CRISPR-Cas systems but CRISPR-specific replicases have not yet been discovered. We have identified and characterised a family of CRISPR-Associated Primase-Polymerases (CAPPs) in a range of prokaryotes that are operonically associated with Cas1 and Cas2. CAPPs belong to the Primase-Polymerase (Prim-Pol) superfamily of replicases that operate in various DNA repair and replication pathways that maintain genome stability. Here, we characterise the DNA synthesis activities of bacterial CAPP homologues from Type IIIA and IIIB CRISPR-Cas systems and establish that they possess a range of replicase activities including DNA priming, polymerisation and strand-displacement. We demonstrate that CAPPs operonically-associated partners, Cas1 and Cas2, form a complex that possesses spacer integration activity. We show that CAPPs physically associate with the Cas proteins to form bespoke CRISPR-Cas complexes. Finally, we propose how CAPPs activities, in conjunction with their partners, may function to undertake key roles in CRISPR-Cas adaptation. CAPPs are putative Primase-Polymerases associated with CRISPR-Cas operons. Here, the authors show CAPPs genetic and physical association with Cas1 and Cas2, their capacity to function as DNA-dependent DNA primases and DNA polymerases, and that Cas1-Cas2 complex adjacent to CAPP has bona fide spacer integration activity.

Citovat

ZABRADY, Katerina, Matej ZABRADY, Peter KOLESÁR, Arthur W. H. LI and Aidan J. DOHERTY. CRISPR-Associated Primase-Polymerases are implicated in prokaryotic CRISPR-Cas adaptation. Nature Communications. London: Nature Publishing Group, 2021, vol. 12, No 1, p. 3690-3707. ISSN 2041-1723. Available from: https://dx.doi.org/10.1038/s41467-021-23535-9.

@article{1823537,
   author = {Zabrady, Katerina and Zabrady, Matej and Kolesár, Peter and Li, Arthur W. H. and Doherty, Aidan J.},
   article_location = {London},
   article_number = {1},
   doi = {http://dx.doi.org/10.1038/s41467-021-23535-9},
   keywords = {CRISPR-Cas systems; DNA; DNA repair enzymes; Enzyme mechanisms},
   language = {eng},
   issn = {2041-1723},
   journal = {Nature Communications},
   title = {CRISPR-Associated Primase-Polymerases are implicated in prokaryotic CRISPR-Cas adaptation},
   url = {https://www.nature.com/articles/s41467-021-23535-9},
   volume = {12},
   year = {2021}
}

TY  - JOUR
ID  - 1823537
AU  - Zabrady, Katerina - Zabrady, Matej - Kolesár, Peter - Li, Arthur W. H. - Doherty, Aidan J.
PY  - 2021
TI  - CRISPR-Associated Primase-Polymerases are implicated in prokaryotic CRISPR-Cas adaptation
JF  - Nature Communications
VL  - 12
IS  - 1
SP  - 3690
EP  - 3690
PB  - Nature Publishing Group
SN  - 20411723
KW  - CRISPR-Cas systems
KW  - DNA
KW  - DNA repair enzymes
KW  - Enzyme mechanisms
UR  - https://www.nature.com/articles/s41467-021-23535-9
N2  - CRISPR-Cas pathways provide prokaryotes with acquired "immunity" against foreign genetic elements, including phages and plasmids. Although many of the proteins associated with CRISPR-Cas mechanisms are characterized, some requisite enzymes remain elusive. Genetic studies have implicated host DNA polymerases in some CRISPR-Cas systems but CRISPR-specific replicases have not yet been discovered. We have identified and characterised a family of CRISPR-Associated Primase-Polymerases (CAPPs) in a range of prokaryotes that are operonically associated with Cas1 and Cas2. CAPPs belong to the Primase-Polymerase (Prim-Pol) superfamily of replicases that operate in various DNA repair and replication pathways that maintain genome stability. Here, we characterise the DNA synthesis activities of bacterial CAPP homologues from Type IIIA and IIIB CRISPR-Cas systems and establish that they possess a range of replicase activities including DNA priming, polymerisation and strand-displacement. We demonstrate that CAPPs operonically-associated partners, Cas1 and Cas2, form a complex that possesses spacer integration activity. We show that CAPPs physically associate with the Cas proteins to form bespoke CRISPR-Cas complexes. Finally, we propose how CAPPs activities, in conjunction with their partners, may function to undertake key roles in CRISPR-Cas adaptation. CAPPs are putative Primase-Polymerases associated with CRISPR-Cas operons. Here, the authors show CAPPs genetic and physical association with Cas1 and Cas2, their capacity to function as DNA-dependent DNA primases and DNA polymerases, and that Cas1-Cas2 complex adjacent to CAPP has bona fide spacer integration activity.
ER  -

ZABRADY, Katerina, Matej ZABRADY, Peter KOLESÁR, Arthur W. H. LI and Aidan J. DOHERTY. CRISPR-Associated Primase-Polymerases are implicated in prokaryotic CRISPR-Cas adaptation. \textit{Nature Communications}. London: Nature Publishing Group, 2021, vol.~12, No~1, p.~3690-3707. ISSN~2041-1723. Available from: https://dx.doi.org/10.1038/s41467-021-23535-9.

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