Results 41 to 50 of about 4,319 (202)

C21orf57 is a human homologue of bacterial YbeY proteins [PDF]

, 2017
The product of the human C21orf57 (huYBEY) gene is predicted to be a homologue of the highly conserved YbeY proteins found in nearly all bacteria. We show that, like its bacterial and chloroplast counterparts, the HuYbeY protein is an RNase and that it ...
Babu, Vignesh M.P., Davies, Bryan W., Ferullo, Daniel J., Ghosal, Anubrata, Gruber, Charley C, Jacob, Asha I, Koehrer, Caroline, Vercruysse, Maarten, Walker, Graham C, Yamanaka, Kinrin   +9 more
core   +1 more source

Rapid degradation of mutant SLC25A46 by the ubiquitin-proteasome system results in MFN1/2-mediated hyperfusion of mitochondria. [PDF]

, 2017
SCL25A46 is a mitochondrial carrier protein that surprisingly localizes to the outer membrane and is distantly related to Ugo1. Here we show that a subset of SLC25A46 interacts with mitochondrial dynamics components and the MICOS complex.
Claypool, Steven M, Jen, Joanna C, Koehler, Carla M, Steffen, Janos, Vashisht, Ajay A, Wan, Jijun, Wohlschlegel, James A   +6 more
core   +1 more source

Polyribosome-Dependent Clustering of Membrane-Anchored RNA Degradosomes To Form Sites of mRNA Degradation in Escherichia coli

mBio, 2021
Here, we show that RNase E, RhlB, and PNPase act together as components of the multienzyme RNA degradosome in polyribosome-dependent clustering to form puncta on the inner cytoplasmic membrane.
Lina Hamouche, Leonora Poljak, Agamemnon J. Carpousis   +2 more
doaj   +1 more source

miRNAs as Influencers of Cell-Cell Communication in Tumor Microenvironment [PDF]

, 2020
microRNAs (miRNAs) are small noncoding RNAs that regulate gene expression at the posttranscriptional level, inducing the degradation of the target mRNA or translational repression.
Conti, Ilaria, Laface, Ilaria, Milani, Daniela, Neri, Luca M, Rimondi, Erika, Simioni, Carolina, Varano, Gabriele   +6 more
core   +1 more source

Oocyte Factors Suppress Mitochondrial Polynucleotide Phosphorylase to Remodel the Metabolome and Enhance Reprogramming

Cell Reports, 2015
Oocyte factors not only drive somatic cell nuclear transfer reprogramming but also augment the efficiency and quality of induced pluripotent stem cell (iPSC) reprogramming.
Swea-Ling Khaw, Chua Min-Wen, Cheng-Gee Koh, Bing Lim, Ng Shyh-Chang   +4 more
doaj   +1 more source

Construction of microbial platform for an energy-requiring bioprocess: practical 2′-deoxyribonucleoside production involving a C−C coupling reaction with high energy substrates [PDF]

, 2012
BACKGROUND: Reproduction and sustainability are important for future society, and bioprocesses are one technology that can be used to realize these concepts.
Jun Ogawa, Jun Shima, Makoto Hibi, Mie Sasaki, Nobuyuki Horinouchi, Sakayu Shimizu, Seiichiro Matsumoto, Takafumi Sakai, Takako Kawano   +8 more
core   +1 more source

Polynucleotide phosphorylase regulates multiple virulence factors and the stabilities of small RNAs RsmY/Z in Pseudomonas aeruginosa

Frontiers in Microbiology, 2016
Post-transcriptional regulation enables bacteria to quickly response to environmental stresses. Polynucleotide phosphorylase (PNPase), which contains an N-terminal catalytic core and C-terminal RNA binding KH-S1 domains, is involved in RNA processing ...
Ronghao eChen, Yuding eWeng, Feng eZhu, Yongxin eJin, Chang eLiu, XiaoLei ePan, Bin eXia, Zhihui eCheng, Shouguang eJin, Shouguang eJin, Weihui eWu   +10 more
doaj   +1 more source

Computational evolution of an RNA-binding protein towards enhanced oxidized-RNA binding

Computational and Structural Biotechnology Journal, 2020
The oxidation of RNA has been implicated in the development of many diseases. Among the four ribonucleotides, guanosine is the most susceptible to oxidation, resulting in the formation of 8-oxo-7,8-dihydroguanosine (8-oxoG). Despite the limited knowledge
Juan C. Gonzalez-Rivera, Asuka A. Orr, Sean M. Engels, Joseph M. Jakubowski, Mark W. Sherman, Katherine N. O'Connor, Tomas Matteson, Brendan C. Woodcock, Lydia M. Contreras, Phanourios Tamamis   +9 more
doaj   +1 more source

A Mutation in PNPT1, Encoding Mitochondrial-RNA-Import Protein PNPase, Causes Hereditary Hearing Loss [PDF]

The American Journal of Human Genetics, 2012
A subset of nuclear-encoded RNAs has to be imported into mitochondria for the proper replication and transcription of the mitochondrial genome and, hence, for proper mitochondrial function. Polynucleotide phosphorylase (PNPase or PNPT1) is one of the very few components known to be involved in this poorly characterized process in mammals.
von Ameln, Simon, Wang, Geng, Boulouiz, Redouane, Rutherford, Mark A., Smith, Geoffrey M., Li, Yun, Pogoda, Hans-Martin, Nürnberg, Gudrun, Stiller, Barbara, Volk, Alexander E., Borck, Guntram, Hong, Jason S., Goodyear, Richard J., Abidi, Omar, Nürnberg, Peter, Hofmann, Kay, Richardson, Gu Y. P., Hammerschmidt, Matthias, Moser, Tobias, Wollnik, Bernd, Koehler, Carla M., Teitell, Michael A., Barakat, Abdelhamid, Kubisch, Christian   +23 more
openaire   +3 more sources

Human mitochondrial RNA decay mediated by PNPase–hSuv3 complex takes place in distinct foci [PDF]

Nucleic Acids Research, 2012
RNA decay is usually mediated by protein complexes and can occur in specific foci such as P-bodies in the cytoplasm of eukaryotes. In human mitochondria nothing is known about the spatial organization of the RNA decay machinery, and the ribonuclease responsible for RNA degradation has not been identified.
Borowski, Lukasz S., Dziembowski, Andrzej, Hejnowicz, Monika S., Stepien, Piotr P., Szczesny, Roman J.   +4 more
openaire   +2 more sources