The anoxic plant mitochondrion as a nitrite: NO reductase

Mitochondrion ◽  
2011 ◽  
Vol 11 (4) ◽  
pp. 537-543 ◽  
Author(s):  
Kapuganti J. Gupta ◽  
Abir U. Igamberdiev
Keyword(s):  
Plant Mitochondrion

scholarly journals Multiple trans-splicing events are required to produce a mature nad1 transcript in a plant mitochondrion.

1991 ◽  
Vol 5 (8) ◽  
pp. 1407-1415 ◽  
Author(s):  
P L Conklin ◽  
R K Wilson ◽  
M R Hanson
Keyword(s):  
Plant Mitochondrion ◽  
Trans Splicing

Molecular Biology of the Plant Mitochondrion

2002 ◽  
Vol 21 (2) ◽  
pp. 111-126 ◽  
Author(s):  
Volker Knoop ◽  
Axel Brennicke
Keyword(s):  
Molecular Biology ◽  
Plant Mitochondrion

Phylogenetic origins of the plant mitochondrion based on a comparative analysis of 5S ribosomal RNA sequences

1985 ◽  
Vol 22 (1) ◽  
pp. 46-52 ◽  
Author(s):  
Edward Villanueva ◽  
Kenneth R. Luehrsen ◽  
Jane Gibson ◽  
Nicholas Delihas ◽  
George E. Fox
Keyword(s):  
Comparative Analysis ◽  
Ribosomal Rna ◽  
Rna Sequences ◽  
Plant Mitochondrion ◽  
5S Ribosomal Rna ◽  
Ribosomal Rna Sequences

scholarly journals The Elusive Plant Mitochondrion as a Genetic System

1994 ◽  
Vol 105 (3) ◽  
pp. 775-780 ◽  
Author(s):  
S. Mackenzie ◽  
S. He ◽  
A. Lyznik
Keyword(s):  
Genetic System ◽  
Plant Mitochondrion

scholarly journals Prediction of thioredoxin and glutaredoxin target proteins by identifying reversibly oxidized cysteinyl residues

2010 ◽  
Vol 7 (3) ◽  
pp. 208-218 ◽  
Author(s):  
Hang-mao Lee ◽  
Karl Josef Dietz ◽  
Ralf Hofestädt
Keyword(s):  
Regulatory Network ◽  
Structural Model ◽  
Regulatory Protein ◽  
Recall Rate ◽  
Plant Mitochondrion ◽  
Network Construction ◽  
Target Proteins ◽  
The Public ◽  
Protein Functions ◽  
Redox Transitions

Summary A significant part of cellular proteins undergo reversible thiol-dependent redox transitions which often control or switch protein functions. Thioredoxins and glutaredoxins constitute two key players in this redox regulatory protein network. Both interact with various categories of proteins containing reversibly oxidized cysteinyl residues. The identification of thioredoxin/glutaredoxin target proteins is a critical step in constructing the redox regulatory network of cells or subcellular compartments. Due to the scarcity of thioredoxin/glutaredoxin target protein records in the public database, a tool called Reversibly Oxidized Cysteine Detector (ROCD) is implemented here to identify potential thioredoxin/glutaredoxin target proteins computationally, so that the in silico construction of redox regulatory network may become feasible. ROCD was tested on 46 thioredoxin target proteins in plant mitochondrion, and the recall rate was 66.7% when 50% sequence identity was chosen for structural model selection. ROCD will be used to predict the thioredoxin/glutaredoxin target proteins in human liver mitochondrion for our redox regulatory network construction project. The ROCD will be developed further to provide prediction with more reliability and incorporated into biological network visualization tools as a node prediction component. This work will advance the capability of traditional database- or text mining-based method in the network construction.

scholarly journals Die Proteinausstattung eines einzelnen pflanzlichen Mitochondriums

BIOspektrum ◽  
2021 ◽  
Vol 27 (7) ◽  
pp. 715-718
Author(s):  
Tatjana Hildebrandt ◽  
Etienne Meyer ◽  
Markus Schwarzländer
Keyword(s):  
Thought Experiment ◽  
Structure And Function ◽  
Single Plant ◽  
Plant Mitochondrion ◽  
Copy Numbers ◽  
Proteomic Approach ◽  
And Function ◽  
Operational Unit

AbstractThe structure and function of mitochondria have been characterized with increasing precision. How the protein inventory defines the characteristics of the organelle remains insufficiently understood, however. Recently we devised a quantitative proteomic approach to estimate the copy numbers of proteins in a single plant mitochondrion, as physical operational unit in the cell. We illustrate how such a simple thought experiment can give fascinating insights into how a mitochondrion works.

scholarly journals cis Recognition Elements in Plant Mitochondrion RNA Editing

2001 ◽  
Vol 21 (20) ◽  
pp. 6731-6737 ◽  
Author(s):  
Jean-Claude Farré ◽  
Gabriel Leon ◽  
Xavier Jordana ◽  
Alejandro Araya
Keyword(s):  
Rna Editing ◽  
Nearest Neighbor ◽  
Mitochondrial Gene ◽  
Plant Mitochondria ◽  
Editing Site ◽  
Higher Plant ◽  
Plant Mitochondrion ◽  
Directed Mutation ◽  
Recognition Elements ◽  
Editing Process

ABSTRACT RNA editing in higher plant mitochondria modifies mRNA sequences by means of C-to-U conversions at highly specific sites. To determine thecis elements involved in recognition of an editing site in plant mitochondria, deletion and site-directed mutation constructs containing the cognate cox II mitochondrial gene were introduced into purified mitochondria by electroporation. The RNA editing status was analyzed for precursor and spliced transcripts from the test construct. We found that only a restricted number of nucleotides in the vicinity of the target C residue were necessary for recognition by the editing machinery and that the nearest neighbor 3′ residues were crucial for the editing process. We provide evidence that two functionally distinguishable sequences can be defined: the 16-nucleotide 5′ region, which can be replaced with the same region from another editing site, and a 6-nucleotide 3′ region specific to the editing site. The latter region may play a role in positioning the actual editing residue.

scholarly journals On the evolutionary origin of the plant mitochondrion and its genome

1989 ◽  
Vol 86 (7) ◽  
pp. 2267-2271 ◽  
Author(s):  
M. W. Gray ◽  
R. Cedergren ◽  
Y. Abel ◽  
D. Sankoff
Keyword(s):  
Evolutionary Origin ◽  
Plant Mitochondrion
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