Structure basis for RNA-guided DNA degradation by Cascade and Cas3

Xiao, Y., Luo, M., Dolan, A. E., Liao, M., Ke, A.
American Association for the Advancement of Science (AAAS)
Published 2018
Publication Date:
2018-07-06
Publisher:
American Association for the Advancement of Science (AAAS)
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
Chemistry and Pharmacology
Geosciences
Computer Science
Medicine
Natural Sciences in General
Physics
Keywords:
Biochemistry, Online Only
Published by:
_version_ 1836399000254676993
autor Xiao, Y., Luo, M., Dolan, A. E., Liao, M., Ke, A.
beschreibung Type I CRISPR-Cas system features a sequential target-searching and degradation process on double-stranded DNA by the RNA-guided Cascade (CRISPR associated complex for antiviral defense) complex and the nuclease-helicase fusion enzyme Cas3, respectively. Here, we present a 3.7-angstrom-resolution cryo–electron microscopy (cryo-EM) structure of the Type I-E Cascade/R-loop/Cas3 complex, poised to initiate DNA degradation. Cas3 distinguishes Cascade conformations and only captures the R-loop–forming Cascade, to avoid cleaving partially complementary targets. Its nuclease domain recruits the nontarget strand (NTS) DNA at a bulged region for the nicking of single-stranded DNA. An additional 4.7-angstrom-resolution cryo-EM structure captures the postnicking state, in which the severed NTS retracts to the helicase entrance, to be threaded for adenosine 5'-triphosphate–dependent processive degradation. These snapshots form the basis for understanding RNA-guided DNA degradation in Type I-E CRISPR-Cas systems.
citation_standardnr 6300149
datenlieferant ipn_articles
feed_id 25
feed_publisher American Association for the Advancement of Science (AAAS)
feed_publisher_url http://www.aaas.org/
insertion_date 2018-07-06
journaleissn 1095-9203
journalissn 0036-8075
publikationsjahr_anzeige 2018
publikationsjahr_facette 2018
publikationsjahr_intervall 7984:2015-2019
publikationsjahr_sort 2018
publisher American Association for the Advancement of Science (AAAS)
quelle Science
relation http://science.sciencemag.org/cgi/content/short/361/6397/eaat0839?rss=1
schlagwort Biochemistry, Online Only
search_space articles
shingle_author_1 Xiao, Y., Luo, M., Dolan, A. E., Liao, M., Ke, A.
shingle_author_2 Xiao, Y., Luo, M., Dolan, A. E., Liao, M., Ke, A.
shingle_author_3 Xiao, Y., Luo, M., Dolan, A. E., Liao, M., Ke, A.
shingle_author_4 Xiao, Y., Luo, M., Dolan, A. E., Liao, M., Ke, A.
shingle_catch_all_1 Structure basis for RNA-guided DNA degradation by Cascade and Cas3
Biochemistry, Online Only
Type I CRISPR-Cas system features a sequential target-searching and degradation process on double-stranded DNA by the RNA-guided Cascade (CRISPR associated complex for antiviral defense) complex and the nuclease-helicase fusion enzyme Cas3, respectively. Here, we present a 3.7-angstrom-resolution cryo–electron microscopy (cryo-EM) structure of the Type I-E Cascade/R-loop/Cas3 complex, poised to initiate DNA degradation. Cas3 distinguishes Cascade conformations and only captures the R-loop–forming Cascade, to avoid cleaving partially complementary targets. Its nuclease domain recruits the nontarget strand (NTS) DNA at a bulged region for the nicking of single-stranded DNA. An additional 4.7-angstrom-resolution cryo-EM structure captures the postnicking state, in which the severed NTS retracts to the helicase entrance, to be threaded for adenosine 5'-triphosphate–dependent processive degradation. These snapshots form the basis for understanding RNA-guided DNA degradation in Type I-E CRISPR-Cas systems.
Xiao, Y., Luo, M., Dolan, A. E., Liao, M., Ke, A.
American Association for the Advancement of Science (AAAS)
0036-8075
00368075
1095-9203
10959203
shingle_catch_all_2 Structure basis for RNA-guided DNA degradation by Cascade and Cas3
Biochemistry, Online Only
Type I CRISPR-Cas system features a sequential target-searching and degradation process on double-stranded DNA by the RNA-guided Cascade (CRISPR associated complex for antiviral defense) complex and the nuclease-helicase fusion enzyme Cas3, respectively. Here, we present a 3.7-angstrom-resolution cryo–electron microscopy (cryo-EM) structure of the Type I-E Cascade/R-loop/Cas3 complex, poised to initiate DNA degradation. Cas3 distinguishes Cascade conformations and only captures the R-loop–forming Cascade, to avoid cleaving partially complementary targets. Its nuclease domain recruits the nontarget strand (NTS) DNA at a bulged region for the nicking of single-stranded DNA. An additional 4.7-angstrom-resolution cryo-EM structure captures the postnicking state, in which the severed NTS retracts to the helicase entrance, to be threaded for adenosine 5'-triphosphate–dependent processive degradation. These snapshots form the basis for understanding RNA-guided DNA degradation in Type I-E CRISPR-Cas systems.
Xiao, Y., Luo, M., Dolan, A. E., Liao, M., Ke, A.
American Association for the Advancement of Science (AAAS)
0036-8075
00368075
1095-9203
10959203
shingle_catch_all_3 Structure basis for RNA-guided DNA degradation by Cascade and Cas3
Biochemistry, Online Only
Type I CRISPR-Cas system features a sequential target-searching and degradation process on double-stranded DNA by the RNA-guided Cascade (CRISPR associated complex for antiviral defense) complex and the nuclease-helicase fusion enzyme Cas3, respectively. Here, we present a 3.7-angstrom-resolution cryo–electron microscopy (cryo-EM) structure of the Type I-E Cascade/R-loop/Cas3 complex, poised to initiate DNA degradation. Cas3 distinguishes Cascade conformations and only captures the R-loop–forming Cascade, to avoid cleaving partially complementary targets. Its nuclease domain recruits the nontarget strand (NTS) DNA at a bulged region for the nicking of single-stranded DNA. An additional 4.7-angstrom-resolution cryo-EM structure captures the postnicking state, in which the severed NTS retracts to the helicase entrance, to be threaded for adenosine 5'-triphosphate–dependent processive degradation. These snapshots form the basis for understanding RNA-guided DNA degradation in Type I-E CRISPR-Cas systems.
Xiao, Y., Luo, M., Dolan, A. E., Liao, M., Ke, A.
American Association for the Advancement of Science (AAAS)
0036-8075
00368075
1095-9203
10959203
shingle_catch_all_4 Structure basis for RNA-guided DNA degradation by Cascade and Cas3
Biochemistry, Online Only
Type I CRISPR-Cas system features a sequential target-searching and degradation process on double-stranded DNA by the RNA-guided Cascade (CRISPR associated complex for antiviral defense) complex and the nuclease-helicase fusion enzyme Cas3, respectively. Here, we present a 3.7-angstrom-resolution cryo–electron microscopy (cryo-EM) structure of the Type I-E Cascade/R-loop/Cas3 complex, poised to initiate DNA degradation. Cas3 distinguishes Cascade conformations and only captures the R-loop–forming Cascade, to avoid cleaving partially complementary targets. Its nuclease domain recruits the nontarget strand (NTS) DNA at a bulged region for the nicking of single-stranded DNA. An additional 4.7-angstrom-resolution cryo-EM structure captures the postnicking state, in which the severed NTS retracts to the helicase entrance, to be threaded for adenosine 5'-triphosphate–dependent processive degradation. These snapshots form the basis for understanding RNA-guided DNA degradation in Type I-E CRISPR-Cas systems.
Xiao, Y., Luo, M., Dolan, A. E., Liao, M., Ke, A.
American Association for the Advancement of Science (AAAS)
0036-8075
00368075
1095-9203
10959203
shingle_title_1 Structure basis for RNA-guided DNA degradation by Cascade and Cas3
shingle_title_2 Structure basis for RNA-guided DNA degradation by Cascade and Cas3
shingle_title_3 Structure basis for RNA-guided DNA degradation by Cascade and Cas3
shingle_title_4 Structure basis for RNA-guided DNA degradation by Cascade and Cas3
timestamp 2025-06-30T23:36:00.434Z
titel Structure basis for RNA-guided DNA degradation by Cascade and Cas3
titel_suche Structure basis for RNA-guided DNA degradation by Cascade and Cas3
topic W
V
TE-TZ
SQ-SU
WW-YZ
TA-TD
U
uid ipn_articles_6300149