Results 41 to 50 of about 3,043 (149)

Architecture and Function of the Human Endonucleases RNase P and RNase MRP [PDF]

IUBMB Life, 2000
AbstractIn the past decade, important advances have been made in our knowledge of the composition of human RNase MRP and RNase P complexes. Both ribonucleoprotein particles function as endonucleases and contain RNA components that are structurally related.
Eenennaam, H. van, Jarrous, N., Venrooij, W.J.W. van, Pruijn, G.J.M.   +3 more
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RNase MRP and disease

WIREs RNA, 2010
AbstractThe human RNase MRP complex consists of a catalytic RNA and several protein components. RNase MRP is a ubiquitously expressed eukaryotic endoribonuclease that cleaves various RNAs, including ribosomal, messenger, and mitochondrial RNAs, in a highly specific fashion.
Mattijssen, S., Welting, T.J.M., Pruijn, G.J.M., Pruijn, G.J.M.   +3 more
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ABC transportome inventory of human pathogenic yeast Candida glabrata: Phylogenetic and expression analysis. [PDF]

PLoS ONE, 2018
ATP-binding cassette (ABC) is one of the two major superfamilies of transporters present across the evolutionary scale. ABC superfamily members came to prominence due to their ability to extrude broad spectrum of substrates and to confer multi drug ...
Sonam Kumari, Mohit Kumar, Nitesh Kumar Khandelwal, Priya Kumari, Mahendra Varma, Poonam Vishwakarma, Garima Shahi, Suman Sharma, Andrew M Lynn, Rajendra Prasad, Naseem A Gaur, Naseem A Gaur   +11 more
doaj   +1 more source

Alba-domain proteins of Trypanosoma brucei are cytoplasmic RNA-binding proteins that interact with the translation machinery. [PDF]

PLoS ONE, 2011
Trypanosoma brucei and related pathogens transcribe most genes as polycistronic arrays that are subsequently processed into monocistronic mRNAs. Expression is frequently regulated post-transcriptionally by cis-acting elements in the untranslated regions (
Jan Mani, Andreas Güttinger, Bernd Schimanski, Manfred Heller, Alvaro Acosta-Serrano, Pascale Pescher, Gerald Späth, Isabel Roditi   +7 more
doaj   +1 more source

Identity of the RNase MRP– and RNase P–associated Th/To autoantigen [PDF]

Arthritis & Rheumatism, 2002
AbstractObjectiveTo characterize the molecular identity of the Th/To autoantigen, which is targeted by autoantibodies in scleroderma and which is associated with the human RNase MRP and RNase P ribonucleoprotein complexes.MethodsProteins immunoprecipitated by anti‐Th/To+ patient antisera from biotinylated total HeLa cell extracts were analyzed by ...
Eenennaam, H. van, Vogelzangs, J.H.P., Lugtenberg, T.M., Hoogen, F.H.J. van den, Venrooij, W.J.W. van, Pruijn, G.J.M.   +5 more
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RNase MRP and RNase P share a common substrate

Nucleic Acids Research, 1993
RNase MRP is a site-specific ribonucleoprotein endoribonuclease that processes RNA from the mammalian mitochondrial displacement loop containing region. RNase P is a site-specific ribonucleoprotein endoribonuclease that processes pre-tRNAs to generate their mature 5'-ends.
T, Potuschak, W, Rossmanith, R, Karwan
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Footprinting analysis of interactions between the largest eukaryotic RNase P/MRP protein Pop1 and RNase P/MRP RNA components [PDF]

RNA, 2015
Ribonuclease (RNase) P and RNase MRP are closely related catalytic ribonucleoproteins involved in the metabolism of a wide range of RNA molecules, including tRNA, rRNA, and some mRNAs. The catalytic RNA component of eukaryotic RNase P retains the core elements of the bacterial RNase P ribozyme; however, the peripheral RNA elements responsible for the ...
Fagerlund, Robert D., Perederina, Anna, Berezin, Igor, Krasilnikov, Andrey S.   +3 more
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Footprinting analysis demonstrates extensive similarity between eukaryotic RNase P and RNase MRP holoenzymes [PDF]

RNA, 2008
Eukaryotic ribonuclease (RNase) P and RNase MRP are evolutionary related RNA-based enzymes involved in metabolism of various RNA molecules, including tRNA and rRNA. In contrast to the closely related eubacterial RNase P, which is comprised of an RNA component and a single small protein, these enzymes contain multiple protein components.
Olga, Esakova, Anna, Perederina, Chao, Quan, Mark E, Schmitt, Andrey S, Krasilnikov   +4 more
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RNase MRP/RNase P: a structure‐function relation conserved in evolution? [PDF]

FEBS Letters, 1993
RNase P and RNase MRP are related ribonucleoproteins. RNase MRP processes mitochondrial precursor‐ (primer) RNAs, whereas RNase P cleaves precursor‐tRNAs to produce their mature 5'‐ends. Both RNase P and RNase MRP are associated with the Th/To ribonucleoprotein suggesting possible interrelated pathways and/or functions.
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hPop5, a Protein Subunit of the Human RNase MRP and RNase P Endoribonucleases [PDF]

Journal of Biological Chemistry, 2001
The RNase MRP and RNase P particles both function as endoribonucleases. RNase MRP has been implicated in the processing of precursor-rRNA, whereas RNase P has been shown to function in the processing of pre-tRNA. Both ribonucleoprotein particles have an RNA component that can be folded into a similar secondary structure and share several protein ...
Eenennaam, H. van, Lugtenberg, T.M., Vogelzangs, J.H.P., Venrooij, W.J.W. van, Pruijn, G.J.M.   +4 more
openaire   +3 more sources