The main regulatory region of mammalian mitochondrial DNA: Structure-function model and evolutionary pattern

1991 ◽  
Vol 33 (1) ◽  
pp. 83-91 ◽  
Author(s):  
Cecilia Saccone ◽  
Graziano Pesole ◽  
Elisabetta Sbisá
Keyword(s):  
Mitochondrial Dna ◽  
Structure Function ◽  
Regulatory Region ◽  
Dna Structure ◽  
Function Model ◽  
Evolutionary Pattern

Phycobilisomes; a Structure-Function Model

2018 ◽  
pp. 9-24
Author(s):  
Robert MacColl ◽  
Deborah Guard-Friar
Keyword(s):  
Structure Function ◽  
Function Model

Workshop no. 6. Structure, function and evolution of kinetoplast DNA

Parasitology ◽  
1981 ◽  
Vol 82 (4) ◽  
pp. 81-93 ◽  
Keyword(s):  
Mitochondrial Dna ◽  
Structure Function ◽  
Network Structure ◽  
The Other ◽  
Kinetoplast Dna ◽  
Base Pairs ◽  
Other Hand

The kinetoplast DNA (kDNA) of kinetoplastidae was the first mitochondrial DNA (mtDNA) to be discovered, and with its unusual network structure, consisting of more than 104catenated DNA circles, it is without equal in nature. Analysis of networks from various genera (reviewed by Borst & Hoeijmakers (1979a) and Englund (1980)) has shown that they always consist of two components: mini-circles and maxi-circles (see Table 1). The mini-circles are the major component and deterraine the size and sliape of networks. They vary in size between 1 and 3 kilo-base pairs (kb = 1000 base pairs (bp)), they are heterogeneous in sequence, their sequence evolves rapidly and their function is not yet known. The maxi-circles, on the other hand, are homogeneous in sequence, their sequence is conserved and they probably represent the counterpart of mtDNA in other organisms.

Mitochondrial DNA structure and function

2002 ◽  
pp. 3-23 ◽  
Author(s):  
Carlos T. Moraes ◽  
Sarika Srivastava ◽  
Ilias Kirkinezos ◽  
Jose Oca-Cossio ◽  
Corina vanWaveren ◽  
...  
Keyword(s):  
Mitochondrial Dna ◽  
Dna Structure ◽  
Structure And Function ◽  
And Function

Profound Length Heteroplasmic Alterations in Mitochondrial DNA Control Region From Primary AML Cells: Implication of Impaired Mitochondrial Replication and Demonstration of ‘vicious cycle’ Hypothesis.

Blood ◽  
2009 ◽  
Vol 114 (22) ◽  
pp. 3116-3116
Author(s):  
Myung-Geun Shin ◽  
Hye Ran Kim ◽  
Hyeoung-Joon Kim ◽  
Hoon Kook ◽  
Tai Ju Hwang ◽  
...  
Keyword(s):  
Mitochondrial Dna ◽  
Control Region ◽  
Copy Number ◽  
Regulatory Region ◽  
Mtdna Control Region ◽  
Vicious Cycle ◽  
Mtdna Copy Number ◽  
Length Heteroplasmy ◽  
Region Length ◽  
D Loop

Abstract Abstract 3116 Poster Board III-53 Mitochondrial DNA (mtDNA) control region (displacement (D)-loop including HV1 and HV2) is a non-coding region of 1124 bp (nucleotide positions, np 16 024–576), which acts as a promoter for both the heavy and light strands of mtDNA, and contains essential transcription and replication elements (Blood 2004;103:4466-77). Importantly, mutations in the D-loop regulatory region might change mtDNA replication rate by modifying the binding affinity of significant trans-activating factors (Eur J Cancer 2004;40:2519-24). Thus, length heteroplasmic alterations of mtDNA control region may be related with mitochondrial dysfunction resulting in ‘vicious cycle’ (Mol Med Today 2000;6:425-32). In an attempt to investigate profiling of mtDNA length heteroplasmic alterations in primary AML cells, we carried out a quantitative size-based PCR product separation by capillary electrophoresis (ABI 3130XL Genetic Analyzer and ABI Prism Genotyper version 3.1) using six targets (np 303-315 poly C, np 16184-16193 poly C, np 514-511 CA repeats, np 3566-3572 poly C, np 12385-12391 poly C and np 12418-12426 poly A). Length heteroplasmy was further confirmed by cloning and sequencing. Quantitative analysis of mtDNA molecules was performed using the QuantiTect SYBR Green PCR kit (Qiagen) and Rotor-Gene 3000 (Corbett Research). Forty-eight AML bone marrow samples were collected after receiving Institutional Review Board approval and informed consent. There were profound alterations of mtGI in 303 poly C, 16184 poly C and 514 CA repeats. The length heteroplasmy pattern of 303 poly C tract in the HV2 region disclosed mixture of 7C, 8C, 9C and 10C mtDNA types. In the HV2 region, length heteroplasmy in poly-C tract at np 303 - 309 exhibited 5 variant peak patterns: 7CT6C+8CT6C (50.0%), 8CT6C+9CT6C (14.0%), 8CT6C+ 9CT6C+ 10CT6C (10.4%), 9CT6C+10CT6C+11CT6C (8.3%) 9CT6C + 10CT6C + 11CT6C+12CT6C (2.1%). The length heteroplasmy pattern of 514-523 CA repeats in the HV2 region exhibited 2 variant peak patterns: CACACACACA (56.3%) and CACACACA (43.7%). In the HV1 region, length heteroplasmy in the poly-C tract at np 16184 - 16193 exhibited 9 variant peak patterns: 5CT4C+5CT3C (31.0%), 6CT4C+6CT3C (2.1%), 9C+10C+11C+12C (16.7%), 9C+10C+11C (2.1%), T4CT4C+5CT3C (4.2%), 9C+10C+11C+12C+13C (2.1%), 3CTC4C+5CT3C (2.1%), 10C+11C+12C+13C (4.2%), 8C+9C+10+11C (2.1%). Primary AML cells revealed decreased enzyme activity in respiratory chain complex I, II and III. AML cells had about a two-fold decrease in mtDNA copy number compared with normal blood mononuclear cells. Current study demonstrates that profound length heteroplasmic alterations in mtDNA control region of primary AML cells may lead to impairment of mitochondrial biogenesis (reduction of mtDNA copy number) and derangement of mitochondrial ATP synthesis. During this perturbation, mitochondria in primary AML cells might produce a large amount of reactive oxygen species, which causes the vicious cycle observed in chronic inflammatory diseases and cancers as well. Disclosures No relevant conflicts of interest to declare.

scholarly journals New Plasmid System To Select forSaccharomyces cerevisiae Purine-Cytosine Permease Affinity Mutants

2001 ◽  
Vol 183 (14) ◽  
pp. 4386-4388 ◽  
Author(s):  
Renaud Wagner ◽  
Marie-Laure Straub ◽  
Jean-Luc Souciet ◽  
Serge Potier ◽  
Jacky de Montigny
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acids ◽  
Structure Function ◽  
Active Transport ◽  
Function Model

ABSTRACT The FCY2 gene of Saccharomyces cerevisiaeencodes a purine-cytosine permease (PCP) that mediates the active transport of purines and cytosine. A structure-function model for this PCP has been recently proposed. In this study, we developed a plasmid-based system that generated a number of affinity-mutated alleles, enabling us to define new amino acids critical for permease function.

HPr: a model protein

1995 ◽  
Vol 73 (5-6) ◽  
pp. 219-222
Author(s):  
J. W. Anderson
Keyword(s):  
Structure Function ◽  
Active Center ◽  
Active Site ◽  
Central Component ◽  
Active Site Residue ◽  
Phosphotransferase System ◽  
Function Model ◽  
Model Protein

Histidine-containing protein (HPr) is a central component of the bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS). This brief review covers recent structure–function studies on the active center of this protein: the role of the active center residues in phosphotransfer; the residues contributing to the phosphohydrolysis properties of HPr; and the contribution residues in HPr make to the pKaof the transiently phosphorylated active-site residue, His 15. As well, the potential for HPr to be used as a model protein for studying problems not directly associated with its function in the PTS is discussed.Key words: phosphoenolpyruvate: sugar phosphotransferase system, histidine-containing protein, active center, structure–function, model protein.

scholarly journals Unusual DNA structure in the regulatory region of the human papovavirus JC virus.

1988 ◽  
Vol 62 (3) ◽  
pp. 922-931 ◽  
Author(s):  
S Amirhaeri ◽  
F Wohlrab ◽  
E O Major ◽  
R D Wells
Keyword(s):  
Jc Virus ◽  
Regulatory Region ◽  
Dna Structure ◽  
Human Papovavirus
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