scholarly journals RNase P protein subunit Rpp29 represses histone H3.3 nucleosome deposition

2016 ◽  
Vol 27 (7) ◽  
pp. 1154-1169 ◽  
Author(s):  
Alyshia Newhart ◽  
Sara Lawrence Powers ◽  
Prashanth Krishna Shastrula ◽  
Isabel Sierra ◽  
Lucy M. Joo ◽  
...  
Keyword(s):  
Chromatin Remodeling ◽  
Antisense Rna ◽  
Rnase P ◽  
Protein Subunit ◽  
P Protein ◽  
Histone H3.3 ◽  
Single Living Cells ◽  
Rna Complex ◽  
Nucleolar Rna ◽  
Single Living

In mammals, histone H3.3 is a critical regulator of transcription state change and heritability at both euchromatin and heterochromatin. The H3.3-specific chaperone, DAXX, together with the chromatin-remodeling factor, ATRX, regulates H3.3 deposition and transcriptional silencing at repetitive DNA, including pericentromeres and telomeres. However, the events that precede H3.3 nucleosome incorporation have not been fully elucidated. We previously showed that the DAXX-ATRX-H3.3 pathway regulates a multi-copy array of an inducible transgene that can be visualized in single living cells. When this pathway is impaired, the array can be robustly activated. H3.3 is strongly recruited to the site during activation where it accumulates in a complex with transcribed sense and antisense RNA, which is distinct from the DNA/chromatin. This suggests that transcriptional events regulate H3.3 recruited to its incorporation sites. Here we report that the nucleolar RNA proteins Rpp29, fibrillarin, and RPL23a are also components of this H3.3/RNA complex. Rpp29 is a protein subunit of RNase P. Of the other subunits, POP1 and Rpp21 are similarly recruited suggesting that a variant of RNase P regulates H3.3 chromatin assembly. Rpp29 knockdown increases H3.3 chromatin incorporation, which suggests that Rpp29 represses H3.3 nucleosome deposition, a finding with implications for epigenetic regulation.

scholarly journals Yeast mitochondrial RNase P RNA synthesis is altered in an RNase P protein subunit mutant: insights into the biogenesis of a mitochondrial RNA-processing enzyme.

1996 ◽  
Vol 16 (7) ◽  
pp. 3429-3436 ◽  
Author(s):  
V Stribinskis ◽  
G J Gao ◽  
P Sulo ◽  
Y L Dang ◽  
N C Martin
Keyword(s):  
Rna Processing ◽  
Mitochondrial Protein ◽  
Rnase P ◽  
Mitochondrial Rna ◽  
Wild Type ◽  
Protein Subunit ◽  
Mitochondrial Trna ◽  
P Deficiency ◽  
F Gene ◽  
P Protein

Rpm2p is a protein subunit of Saccharomyces cerevisiae yeast mitochondrial RNase P, an enzyme which removes 5' leader sequences from mitochondrial tRNA precursors. Precursor tRNAs accumulate in strains carrying a disrupted allele of RPM2. The resulting defect in mitochondrial protein synthesis causes petite mutants to form. We report here that alteration in the biogenesis of Rpm1r, the RNase P RNA subunit, is another consequence of disrupting RPM2. High-molecular-weight transcripts accumulate, and no mature Rpm1r is produced. Transcript mapping reveals that the smallest RNA accumulated is extended on both the 5' and 3' ends relative to mature Rpm1r. This intermediate and other longer transcripts which accumulate are also found as low-abundance RNAs in wild-type cells, allowing identification of processing events necessary for conversion of the primary transcript to final products. Our data demonstrate directly that Rpm1r is transcribed with its substrates, tRNA met f and tRNAPro, from a promoter located upstream of the tRNA met f gene and suggest that a portion also originates from a second promoter, located between the tRNA met f gene and RPM1. We tested the possibility that precursors accumulate because the RNase P deficiency prevents the removal of the downstream tRNAPro. Large RPM1 transcripts still accumulate in strains missing this tRNA. Thus, an inability to process cotranscribed tRNAs does not explain the precursor accumulation phenotype. Furthermore, strains with mutant RPM1 genes also accumulate precursor Rpm1r, suggesting that mutations in either gene can lead to similar biogenesis defects. Several models to explain precursor accumulation are presented.

scholarly journals Influence of Conformation of M. tuberculosis RNase P Protein Subunit on Its Function

PLoS ONE ◽  
2016 ◽  
Vol 11 (4) ◽  
pp. e0153798 ◽  
Author(s):  
Alla Singh ◽  
Shah Ubaid-ullah ◽  
Anup K. Ramteke ◽  
Janendra K Batra
Keyword(s):  
Rnase P ◽  
Protein Subunit ◽  
P Protein

scholarly journals Analysis of RNase P Protein (rnpA) Expression in Bacillus subtilis Utilizing Strains with Suppressible rnpA Expression

2006 ◽  
Vol 188 (19) ◽  
pp. 6816-6823 ◽  
Author(s):  
Markus Gößringer ◽  
Rosel Kretschmer-Kazemi Far ◽  
Roland K. Hartmann
Keyword(s):  
Bacillus Subtilis ◽  
Direct Proof ◽  
Rnase P ◽  
Protein Subunit ◽  
Cell Growth Arrest ◽  
P Protein ◽  
In The Wild ◽  
Arrest Growth ◽  
Protein Variants

ABSTRACT Bacterial RNase P is composed of an RNA subunit and a single protein subunit (encoded by the rnpB and rnpA genes, respectively). We constructed Bacillus subtilis mutant strains that conditionally express the RNase P protein under control of the xylose promoter (P xyl ). In one strain (d7), rnpA expression was efficiently repressed in the absence of the inducer xylose, leading to cell growth arrest. Growth could be restored by a second functional rnpA allele. This is the first RNase P protein knockdown strain, providing the first direct proof that the rnpA gene is essential in B. subtilis and, by inference, in other bacteria. We further show (i) that, in the wild-type context, rnpA expression is attenuated by transcriptional polarity and (ii) that translation of rnpA mRNA in B. subtilis can be initiated at two alternative start codons. His-tagged RNase P protein variants are functional in vivo and permit purification of in vivo-assembled holoenzymes by affinity chromatography. Simultaneous expression of plasmid-encoded RNase P RNA and His-tagged protein increased RNase P holoenzyme yields. Massive overproduction of RNase P protein in strain d7 is compatible with cell viability.

scholarly journals A functional RNase P protein subunit of bacterial origin in some eukaryotes

2011 ◽  
Vol 286 (5-6) ◽  
pp. 359-369 ◽  
Author(s):  
Lien B. Lai ◽  
Pilar Bernal-Bayard ◽  
Gireesha Mohannath ◽  
Stella M. Lai ◽  
Venkat Gopalan ◽  
...  
Keyword(s):  
Rnase P ◽  
Protein Subunit ◽  
Bacterial Origin ◽  
P Protein

scholarly journals By Any Other Name: Heterologous Replacement of the Escherichia coli RNase P Protein Subunit Has In Vivo Fitness Consequences

PLoS ONE ◽  
2012 ◽  
Vol 7 (3) ◽  
pp. e32456 ◽  
Author(s):  
Paula C. G. Turrini ◽  
Jasmine L. Loveland ◽  
Robert L. Dorit
Keyword(s):  
Escherichia Coli ◽  
Rnase P ◽  
Protein Subunit ◽  
P Protein ◽  
Fitness Consequences

Application of FRAP and digitized fluorescence microscopy to problems in cell membrane dynamics

1988 ◽  
Vol 46 ◽  
pp. 118-119
Author(s):  
K. Jacobson ◽  
A. Ishihara ◽  
B. Holifield ◽  
F. Zhang
Keyword(s):  
Fluorescence Microscopy ◽  
Cell Biology ◽  
Extended Period ◽  
Dynamic Structure ◽  
Living Cells ◽  
Membrane Dynamics ◽  
Molecular Cell Biology ◽  
Image Averaging ◽  
Single Living Cells ◽  
Single Living

Our laboratory is concerned with understanding the dynamic structure of the plasma membrane with particular reference to the movement of membrane constituents during cell locomotion. In addition to the standard tools of molecular cell biology, we employ both fluorescence recovery after photo- bleaching (FRAP) and digitized fluorescence microscopy (DFM) to investigate individual cells. FRAP allows the measurement of translational mobility of membrane and cytoplasmic molecules in small regions of single, living cells. DFM is really a new form of light microscopy in that the distribution of individual classes of ions, molecules, and macromolecules can be followed in single, living cells. By employing fluorescent antibodies to defined antigens or fluorescent analogs of cellular constituents as well as ultrasensitive, electronic image detectors and video image averaging to improve signal to noise, fluorescent images of living cells can be acquired over an extended period without significant fading and loss of cell viability.

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