PPR-SMRs: ancient proteins with enigmatic functions

S Liu, J Melonek, LM Boykin, I Small, KA Howell - RNA biology, 2013 - Taylor & Francis
A small subset of the large pentatricopeptide repeat (PPR) protein family in higher plants
contain a C-terminal small MutS-related (SMR) domain. Although few in number, they figure …

A small RNA that regulates motility and biofilm formation in response to changes in nutrient availability in Escherichia coli

MK Thomason, F Fontaine, N De Lay… - Molecular …, 2012 - Wiley Online Library
In bacteria, many small regulatory RNAs (sRNAs) are induced in response to specific
environmental signals or stresses and act by base‐pairing with mRNA targets to affect …

The enigmatic roles of PPR‐SMR proteins in plants

Y Zhang, C Lu - Advanced Science, 2019 - Wiley Online Library
The pentatricopeptide repeat (PPR) protein family, with more than 400 members, is one of
the largest and most diverse protein families in land plants. A small subset of PPR proteins …

PPR-SMR protein SOT1 has RNA endonuclease activity

W Zhou, Q Lu, Q Li, L Wang, S Ding… - Proceedings of the …, 2017 - National Acad Sciences
Numerous attempts have been made to identify and engineer sequence-specific RNA
endonucleases, as these would allow for efficient RNA manipulation. However, no natural …

Structure and function of the small MutS‐related domain

K Fukui, S Kuramitsu - Molecular biology international, 2011 - Wiley Online Library
MutS family proteins are widely distributed in almost all organisms from bacteria to human
and play central roles in various DNA transactions such as DNA mismatch repair and …

A plastid-localized pentatricopeptide repeat protein is required for both pollen development and plant growth in rice

YJ Liu, X Liu, H Chen, P Zheng, W Wang, L Wang… - Scientific reports, 2017 - nature.com
Several mitochondrial-targeted pentatricopeptide repeat (PPR) proteins involved in pollen
development have been reported to be fertility restorer (Rf) proteins. However, the roles of …

The nuclease activities of both the Smr domain and an additional LDLK motif are required for an efficient anti‐recombination function of Helicobacter pylori MutS2

PP Damke, R Dhanaraju, S Marsin… - Molecular …, 2015 - Wiley Online Library
H elicobacter pylori, a human pathogen, is a naturally and constitutively competent bacteria,
displaying a high rate of intergenomic recombination. While recombination events are …

Structural and functional studies of MutS2 from Deinococcus radiodurans

H Zhang, Q Xu, M Lu, X Xu, Y Wang, L Wang, Y Zhao… - DNA repair, 2014 - Elsevier
The MutS2 homologues have been found widespread in most prokaryotes, which are
involved in DNA repair and reactive oxygen species detoxification. The C-terminal small …

Structure-based functional identification of Helicobacter pylori HP0268 as a nuclease with both DNA nicking and RNase activities

KY Lee, KY Lee, JH Kim, IG Lee, SH Lee… - Nucleic acids …, 2015 - academic.oup.com
HP0268 is a conserved, uncharacterized protein from Helicobacter pylori. Here, we
determined the solution structure of HP0268 using three-dimensional nuclear magnetic …

Molecular basis for the functions of a bacterial MutS2 in DNA repair and recombination

G Wang, RJ Maier - DNA repair, 2017 - Elsevier
Bacterial MutS2 proteins, consisting of functional domains for ATPase, DNA-binding, and
nuclease activities, play roles in DNA recombination and repair. Here we observe a …