We purified the Xis protein of the conjugative transposon Tn916 and showed by nuclease protection experiments that Xis bound specifically to sites close to each end of Tn916. These specific binding sites are close to, and in the same relative orientation to, binding sites for the N-terminal domain of Tn916 integrase protein. These results suggest that Xis is involved in the formation of nucleoprotein structures at the ends of Tn916 that help to correctly align the ends so that excision can occur.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC179005 | PMC |
| http://dx.doi.org/10.1128/jb.179.8.2567-2572.1997 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Evolution of the Tn ICE family: -mediated coordination of cargo gene upregulation and horizontal transfer.
Microbiol Spectr
October 2024
Department of Molecular and Chemical Life Sciences, Graduate School of Life Sciences, Tohoku University, Sendai, Japan.
ICETn carries a operon for the mineralization of polychlorinated biphenyls (PCBs)/biphenyl and belongs to the Tn ICE (integrative and conjugative element) family. In this study, we investigated the role of the gene in ICE transfer. The gene encodes a LysR-type transcriptional regulator, which is conserved in sequence, positioning, and directional orientation among Tn family ICEs.
View Article and Find Full Text PDFEmulation of randomized trials of direct oral anticoagulants with claims data and implications for new Factor XI inhibitors.
Pharmacoepidemiol Drug Saf
May 2024
Division of Pharmacoepidemiology, Brigham and Women's Hospital, Boston, Massachusetts, USA.
Direct oral anticoagulants (DOACs) revolutionized the management of thromboembolic disorders. Clinical care may be further improved as Factor XIs undergo large-scale outcome trials. What role can non-randomized database studies play in expediting understanding of these drugs in clinical practice? The RCT-DUPLICATIVE Initiative emulated the design of eight DOAC randomized clinical trials (RCT) using non-randomized claims database studies.
View Article and Find Full Text PDFA nanopore-based cucumber genome assembly reveals structural variations at two QTLs controlling hypocotyl elongation.
Plant Physiol
May 2024
College of Horticulture, Sichuan Agricultural University, 611130 Chengdu, China.
Article Synopsis
- The Xishuangbanna (XIS) cucumber is a unique semiwild variety with distinct agronomic traits, and researchers used Nanopore sequencing technology to assemble a high-quality genome for the landrace XIS49.
- A comparison with the Chinese Long (CL) variety identified over 10,000 structural variations, confirming key traits related to spine, tubercle, and carpel number in XIS49.
- Two quantitative trait loci (QTLs) for hypocotyl elongation under low light were fine-mapped: SH3.1, linked to the Phytochrome B gene, and SH6.1, linked to a zinc finger protein, displaying how specific genetic elements influence cucumber growth in
Bacteriophage lambda site-specific recombination.
Mol Microbiol
May 2024
Department of Molecular Biology, Cell Biology, and Biochemistry, Warren Alpert Medical School, Brown University, Providence, Rhode Island, USA.
The site-specific recombination pathway of bacteriophage λ encompasses isoenergetic but highly directional and tightly regulated integrative and excisive reactions that integrate and excise the vial chromosome into and out of the bacterial chromosome. The reactions require 240 bp of phage DNA and 21 bp of bacterial DNA comprising 16 protein binding sites that are differentially used in each pathway by the phage-encoded Int and Xis proteins and the host-encoded integration host factor and factor for inversion stimulation proteins. Structures of higher-order protein-DNA complexes of the four-way Holliday junction recombination intermediates provided clarifying insights into the mechanisms, directionality, and regulation of these two pathways, which are tightly linked to the physiology of the bacterial host cell.
View Article and Find Full Text PDFThe NMR structure of the Orf63 lytic developmental protein from lambda bacteriophage.
Sci Rep
February 2024
Department of Biology, York University, Toronto, ON, M3J1P3, Canada.
The orf63 gene resides in a region of the lambda bacteriophage genome between the exo and xis genes and is among the earliest genes transcribed during infection. In lambda phage and Shiga toxin (Stx) producing phages found in enterohemorrhagic Escherichia coli (EHEC) associated with food poisoning, Orf63 expression reduces the host survival and hastens the period between infection and lysis thereby giving it pro-lytic qualities. The NMR structure of dimeric Orf63 reveals a fold consisting of two helices and one strand that all make extensive intermolecular contacts.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!