scholarly journals Human RNase P: a tRNA-processing enzyme and transcription factor

2007 ◽  
Vol 35 (11) ◽  
pp. 3519-3524 ◽  
Author(s):  
N. Jarrous ◽  
R. Reiner
Keyword(s):  
Transcription Factor ◽  
Rnase P ◽  
Trna Processing ◽  
Processing Enzyme ◽  
Human Rnase

scholarly journals Unexpected diversity of RNase P, an ancient tRNA processing enzyme: Challenges and prospects

FEBS Letters ◽  
2009 ◽  
Vol 584 (2) ◽  
pp. 287-296 ◽  
Author(s):  
Lien B. Lai ◽  
Agustín Vioque ◽  
Leif A. Kirsebom ◽  
Venkat Gopalan
Keyword(s):  
Rnase P ◽  
Trna Processing ◽  
Processing Enzyme

scholarly journals RNase P without RNA: Identification and Functional Reconstitution of the Human Mitochondrial tRNA Processing Enzyme

Cell ◽  
2008 ◽  
Vol 135 (3) ◽  
pp. 462-474 ◽  
Author(s):  
Johann Holzmann ◽  
Peter Frank ◽  
Esther Löffler ◽  
Keiryn L. Bennett ◽  
Christopher Gerner ◽  
...  
Keyword(s):  
Rnase P ◽  
Mitochondrial Trna ◽  
Trna Processing ◽  
Processing Enzyme

scholarly journals Basic Domains Target Protein Subunits of the RNase MRP Complex to the Nucleolus Independently of Complex Association

2001 ◽  
Vol 12 (11) ◽  
pp. 3680-3689 ◽  
Author(s):  
Hans van Eenennaam ◽  
Annemarie van der Heijden ◽  
Rolf J. R. J. Janssen ◽  
Walther J. van Venrooij ◽  
Ger J. M. Pruijn
Keyword(s):  
Protein Composition ◽  
Rnase P ◽  
Nucleolar Localization ◽  
Rrna Processing ◽  
Protein Subunits ◽  
Trna Processing ◽  
Rnase Mrp ◽  
Human Rnase ◽  
The Difference ◽  
Active Transport Process

The RNase MRP and RNase P ribonucleoprotein particles both function as endoribonucleases, have a similar RNA component, and share several protein subunits. RNase MRP has been implicated in pre-rRNA processing and mitochondrial DNA replication, whereas RNase P functions in pre-tRNA processing. Both RNase MRP and RNase P accumulate in the nucleolus of eukaryotic cells. In this report we show that for three protein subunits of the RNase MRP complex (hPop1, hPop4, and Rpp38) basic domains are responsible for their nucleolar accumulation and that they are able to accumulate in the nucleolus independently of their association with the RNase MRP and RNase P complexes. We also show that certain mutants of hPop4 accumulate in the Cajal bodies, suggesting that hPop4 traverses through these bodies to the nucleolus. Furthermore, we characterized a deletion mutant of Rpp38 that preferentially associates with the RNase MRP complex, giving a first clue about the difference in protein composition of the human RNase MRP and RNase P complexes. On the basis of all available data on nucleolar localization sequences, we hypothesize that nucleolar accumulation of proteins containing basic domains proceeds by diffusion and retention rather than by an active transport process. The existence of nucleolar localization sequences is discussed.

scholarly journals Use of chemical modification and mass spectrometry to identify substrate-contacting sites in proteinaceous RNase P, a tRNA processing enzyme

2016 ◽  
Vol 44 (11) ◽  
pp. 5344-5355 ◽  
Author(s):  
Tien-Hao Chen ◽  
Akiko Tanimoto ◽  
Nikoloz Shkriabai ◽  
Mamuka Kvaratskhelia ◽  
Vicki Wysocki ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Chemical Modification ◽  
Rnase P ◽  
Trna Processing ◽  
Processing Enzyme

scholarly journals Multiple cis-acting elements are required for RNA polymerase III transcription of the gene encoding H1 RNA, the RNA component of human RNase P.

1991 ◽  
Vol 266 (34) ◽  
pp. 22796-22799
Author(s):  
G.J. Hannon ◽  
A. Chubb ◽  
P.A. Maroney ◽  
G. Hannon ◽  
S. Altman ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Iii ◽  
Rnase P ◽  
Gene Encoding ◽  
Cis Acting ◽  
Polymerase Iii ◽  
Human Rnase

scholarly journals Fomites and the environment did not have an important role in COVID-19 transmission in a Brazilian mid-sized city

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Ana Luíza Silva Rocha ◽  
Josilene Ramos Pinheiro ◽  
Thamilin Costa Nakamura ◽  
José Domingos Santos da Silva ◽  
Beatriz Gonçalves Silva Rocha ◽  
...  
Keyword(s):  
Cell Phones ◽  
Rnase P ◽  
Human Cells ◽  
Market Area ◽  
Paper Money ◽  
P Gene ◽  
Human Rnase ◽  
The World ◽  
Reference Hospital

AbstractIt is not clear if COVID-19 can be indirectly transmitted. It is not possible to conclude the role of the environment in transmission of SARS-CoV-2 without studying areas in which people transit in great numbers. In this work we aimed to better understand the role of environment in the spread of COVID-19. We investigated the presence of SARS-CoV-2 in fomites as well as in the air and in the sewage using RT-qPCR. We studied both, a reference market area and a COVID-19 reference hospital at Barreiras city, Brazil. We collected and analyzed a total of 418 samples from mask fronts, cell phones, paper money, card machines, sewage, air and bedding during the ascendant phase of the epidemiological curve of COVID-19 in Barreiras. As a result, we detected the human RNAse P gene in most of samples, which indicates the presence of human cells or their fragments in specimens. However, we did not detect any trace of SARS-CoV-2 in all samples analyzed. We conclude that, so far, the environment and inanimate materials did not have an important role in COVID-19 transmission in Barreiras city. Therefore, similar results can probably be found in other cities, mainly those with COVID-19 epidemiological scenarios similar to that of Barreiras city. Our study is a small piece indicating the possibility that fomites and the environment do not have an important role in COVID-19 transmission. However, further studies are necessary to better understand the world scenario.

scholarly journals Minimal and RNA-free RNase P in Aquifex aeolicus

2017 ◽  
Vol 114 (42) ◽  
pp. 11121-11126 ◽  
Author(s):  
Astrid I. Nickel ◽  
Nadine B. Wäber ◽  
Markus Gößringer ◽  
Marcus Lechner ◽  
Uwe Linne ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Gene Transfer ◽  
Horizontal Gene Transfer ◽  
Rnase P ◽  
Aquifex Aeolicus ◽  
Trna Processing ◽  
Hyperthermophilic Bacterium ◽  
Domains Of Life

RNase P is an essential tRNA-processing enzyme in all domains of life. We identified an unknown type of protein-only RNase P in the hyperthermophilic bacterium Aquifex aeolicus: Without an RNA subunit and the smallest of its kind, the 23-kDa polypeptide comprises a metallonuclease domain only. The protein has RNase P activity in vitro and rescued the growth of Escherichia coli and Saccharomyces cerevisiae strains with inactivations of their more complex and larger endogenous ribonucleoprotein RNase P. Homologs of Aquifex RNase P (HARP) were identified in many Archaea and some Bacteria, of which all Archaea and most Bacteria also encode an RNA-based RNase P; activity of both RNase P forms from the same bacterium or archaeon could be verified in two selected cases. Bioinformatic analyses suggest that A. aeolicus and related Aquificaceae likely acquired HARP by horizontal gene transfer from an archaeon.

scholarly journals Structure and transcription of a human gene for H1 RNA, the RNA component of human RNase P

1990 ◽  
Vol 18 (1) ◽  
pp. 97-103 ◽  
Author(s):  
Madeline Baer ◽  
Timothy W. Nilsen ◽  
Christine Costigan ◽  
Sidney Altman
Keyword(s):  
Human Gene ◽  
Rnase P ◽  
Human Rnase
Sign in / Sign up

Export Citation Format

Share Document