The Protein Component of Bacterial Ribonuclease P Flickers the Metal Ion Response to the Substrate Shape Preference of the Ribozyme

2003 ◽  
Vol 67 (10) ◽  
pp. 2294-2296 ◽  
Author(s):  
Tomoaki ANDO ◽  
Terumichi TANAKA ◽  
Yo KIKUCHI
Keyword(s):  
Metal Ion ◽  
Protein Component ◽  
Ribonuclease P ◽  
Shape Preference

scholarly journals Guide DNA technique reveals that the protein component of bacterial ribonuclease P is a modifier for substrate recognition

FEBS Letters ◽  
2001 ◽  
Vol 491 (1-2) ◽  
pp. 94-98 ◽  
Author(s):  
Terumichi Tanaka ◽  
Hideo Baba ◽  
Yoshiaki Hori ◽  
Yo Kikuchi
Keyword(s):  
Substrate Recognition ◽  
Protein Component ◽  
Ribonuclease P

scholarly journals Protein component of the ribozyme ribonuclease P alters substrate recognition by directly contacting precursor tRNA

1998 ◽  
Vol 95 (26) ◽  
pp. 15212-15217 ◽  
Author(s):  
S. Niranjanakumari ◽  
T. Stams ◽  
S. M. Crary ◽  
D. W. Christianson ◽  
C. A. Fierke
Keyword(s):  
Substrate Recognition ◽  
Protein Component ◽  
Ribonuclease P

scholarly journals Helix P4 is a divalent metal ion binding site in the conserved core of the ribonuclease P ribozyme

RNA ◽  
2000 ◽  
Vol 6 (4) ◽  
pp. 511-519 ◽  
Author(s):  
ERIC L. CHRISTIAN ◽  
NICHOLAS M. KAYE ◽  
MICHAEL E. HARRIS
Keyword(s):  
Binding Site ◽  
Metal Ion ◽  
Divalent Metal ◽  
Ribonuclease P ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Divalent Metal Ion ◽  
Conserved Core

Metal ion requirements and other aspects of the reaction catalyzed by M1 RNA, the RNA subunit of ribonuclease P from Escherichia coli

Biochemistry ◽  
1986 ◽  
Vol 25 (7) ◽  
pp. 1509-1515 ◽  
Author(s):  
Cecilia Guerrier-Takada ◽  
Karen Haydock ◽  
Leland Allen ◽  
Sidney Altman
Keyword(s):  
Escherichia Coli ◽  
Metal Ion ◽  
Ribonuclease P ◽  
M1 Rna

Structural insight into precursor tRNA processing by yeast ribonuclease P

Science ◽  
2018 ◽  
Vol 362 (6415) ◽  
pp. eaat6678 ◽  
Author(s):  
Pengfei Lan ◽  
Ming Tan ◽  
Yuebin Zhang ◽  
Shuangshuang Niu ◽  
Juan Chen ◽  
...  
Keyword(s):  
Metal Ion ◽  
Simulation Analysis ◽  
Reaction Pathway ◽  
Rnase P ◽  
Ribonuclease P ◽  
Measuring Device ◽  
Catalytic Center ◽  
Cryo Electron Microscopy ◽  
Phosphate Backbone ◽  
Protein Components

Ribonuclease P (RNase P) is a universal ribozyme responsible for processing the 5′-leader of pre–transfer RNA (pre-tRNA). Here, we report the 3.5-angstrom cryo–electron microscopy structures of Saccharomyces cerevisiae RNase P alone and in complex with pre-tRNAPhe. The protein components form a hook-shaped architecture that wraps around the RNA and stabilizes RNase P into a “measuring device” with two fixed anchors that recognize the L-shaped pre-tRNA. A universally conserved uridine nucleobase and phosphate backbone in the catalytic center together with the scissile phosphate and the O3′ leaving group of pre-tRNA jointly coordinate two catalytic magnesium ions. Binding of pre-tRNA induces a conformational change in the catalytic center that is required for catalysis. Moreover, simulation analysis suggests a two-metal-ion SN2 reaction pathway of pre-tRNA cleavage. These results not only reveal the architecture of yeast RNase P but also provide a molecular basis of how the 5′-leader of pre-tRNA is processed by eukaryotic RNase P.

The Immuno-Electron Microscopic Localization of the Mo-Fe Protein Component of Nitrogenase in Cells of Azotobacter Vinelandii

1973 ◽  
Vol 31 ◽  
pp. 574-575
Author(s):  
J. T. Stasny ◽  
R. C. Burns ◽  
R. W. F. Hardy
Keyword(s):  
Cellular Localization ◽  
Direct Evidence ◽  
Azotobacter Vinelandii ◽  
Intracellular Localization ◽  
Protein Component ◽  
Electron Microscopic ◽  
Thin Sections ◽  
Fe Protein ◽  
Intracytoplasmic Membranes

Structure-functlon studies of biological N2-fixation have correlated the presence of the enzyme nitrogenase with increased numbers of intracytoplasmic membranes in Azotobacter. However no direct evidence has been provided for the internal cellular localization of any nitrogenase. Recent advances concerned with the crystallizatiorTand the electron microscopic characterization of the Mo-Fe protein component of Azotobacter nitrogenase, prompted the use of this purified protein to obtain antibodies (Ab) to be conjugated to electron dense markers for the intracellular localization of the protein by electron microscopy. The present study describes the use of ferritin conjugated to goat antitMo-Fe protein immunoglobulin (IgG) and the observations following its topical application to thin sections of N2-grown Azotobacter.

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