Redox Potential Regulates Binding of Universal Minicircle Sequence Binding Protein at the Kinetoplast DNA Replication Origin

Onn, Itay; Milman-Shtepel, Neta; Shlomai, Joseph

doi:10.1128/ec.3.2.277-287.2004

Cited by 56 publications

(59 citation statements)

References 79 publications

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“…They are in accord with previous reports showing that many sitespecific DNA-binding proteins bind several target sites on the DNA and self-associate by protein-protein interactions to generate highly organized nucleoprotein structures (35)(36)(37)(38)(39)(40). In this context it is noteworthy that we have previously reported on the high capacity of UMSBP monomers to conduct proteinprotein interactions and to oligomerize in solution (23).…”

Section: Interactions Of Umsbp With Its Two Binding Sites At the Minisupporting

confidence: 92%

“…3, Site 2). This value is similar to the values obtained in our previous analyses using a single-stranded UMS (16,23) or H14 (19) oligonucleotides. The K D value measured for the interaction of UMSBP at the second site (Fig.…”

Section: Interactions Of Umsbp With Its Two Binding Sites At the Minisupporting

confidence: 90%

“…Preliminary observations suggested that UMSBP interacts with several replication proteins. 5 Recent structure-function analyses of UMSBP have revealed that whereas the UMSBP C-terminal domain is involved in the binding of DNA, its N-terminal domain mediates protein-protein interactions (23). The kinetics rates measured here for UMSBP interactions with the minicircle origin sequences (Fig.…”

Section: Discussionmentioning

confidence: 67%

“…Preparation of UMSBP-Cloning of the C. fasciculata UMSBP gene open reading frame (15) and the preparation of pure recombinant UMSBP were conducted as we have previously described (23).…”

Section: Methodsmentioning

confidence: 99%

“…This motif forms a compact zinc finger that has been associated with the binding of single-stranded nucleic acids (20 -22). We have previously reported on the effect of redox on the binding of UMSBP to the origin sequence as well as on the protein oligomerization and suggested that redox potential may play a major role in the regulation of UMSBP action at the replication origin (23). Immunolocalization of UMSBP within the kinetoplast has revealed two distinct protein foci at the kineto-flagellar zone, near the suggested minicircle replication site (24).…”

mentioning

confidence: 98%

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Binding of the Universal Minicircle Sequence Binding Protein at the Kinetoplast DNA Replication Origin

Onn

Kapeller

Abu-Elneel

et al. 2006

Journal of Biological Chemistry

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Kinetoplast DNA, the mitochondrial DNA of trypanosomatids, is a remarkable DNA structure that contains, in the species Crithidia fasciculata, 5000 topologically linked duplex DNA minicircles. Their replication initiates at two conserved sequences, a dodecamer, known as the universal minicircle sequence (UMS), and a hexamer, which are located at the replication origins of the minicircle L and H strands, respectively. A UMS-binding protein (UMSBP) binds specifically the 12-mer UMS sequence and a 14-mer sequence that contains the conserved hexamer in their single-stranded DNA conformation. In vivo cross-linking analyses reveal the binding of UMSBP to kinetoplast DNA networks in the cell. Furthermore, UMSBP binds in vitro to native minicircle origin fragments, carrying the UMSBP recognition sequences. UMSBP binding at the replication origin induces conformational changes in the bound DNA through its folding, aggregation and condensation.Kinetoplast DNA (kDNA) 4 is a unique extrachromosomal DNA found in the single mitochondrion of trypanosomatids. In the species Crithidia fasciculata the kDNA network consists of ϳ5000 duplex DNA minicircles of 2.5 kbp and 50 maxicircles of 37 kbp that are interlocked topologically to form a DNA network (1-5). Maxicircles contain mitochondrial genes, encoding mitochondrial proteins and rRNA. Minicircles encode for guide RNAs that function in the process of mitochondrial mRNA editing (6 -8). Minicircles in most trypanosomatids species are heterogeneous in sequence. However, a few structural and sequence motifs are conserved in all the minicircles within networks of a given species as well as in minicircles of different trypanosomatid species. These include two short sequences that are associated with the process of replication initiation, which are located 70 -100 nucleotides apart in the minicircle molecule; they are the dodecameric sequence GGGGT-TGGTGTA, designated the universal minicircle sequence (UMS) and the hexameric sequence ACGCCC. These sequences have been mapped to the sites of the replication origins of the minicircle light (L) and heavy (H) strands, respectively (for review, see Refs. 1-5). Comparison of the complete minicircle sequences of several species of trypanosomatids reveals that minicircles from different trypanosomatids contain either one (Trypanosoma brucei GenBank TM accession number M15323; Leishmania major, GenBank TM accession number Z32845), two (C. fasciculata, GenBank TM accession number M19266), or three (Trypanosoma cruzi, GenBank TM accession number X56188) copies of the conserved origin region. The two conserved origin regions in C. fasciculata kDNA minicircles are designated OriA and OriB. Each of these origin regions includes the two conserved origin sequences. According to the currently accepted model for kDNA replication, only one of the origins is active during minicircle replication, and the active origin is randomly selected in each replication cycle (9).Unlike the replication of mitochondrial DNA in other eukaryotic cells, which takes place...

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Section: Interactions Of Umsbp With Its Two Binding Sites At the Minisupporting

confidence: 92%

Section: Interactions Of Umsbp With Its Two Binding Sites At the Minisupporting

confidence: 90%

Section: Discussionmentioning

confidence: 67%

“…Preparation of UMSBP-Cloning of the C. fasciculata UMSBP gene open reading frame (15) and the preparation of pure recombinant UMSBP were conducted as we have previously described (23).…”

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 98%

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Binding of the Universal Minicircle Sequence Binding Protein at the Kinetoplast DNA Replication Origin

Onn

Kapeller

Abu-Elneel

et al. 2006

Journal of Biological Chemistry

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In Search of Trypanocidal Drugs

Flohé¹

2009

Antiparasitic and Antibacterial Drug Discovery

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Survey of the year 2004 commercial optical biosensor literature

Rich

Myszka

2005

J of Molecular Recognition

114

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The year 2004 represents a milestone for the biosensor research community: in this year, over 1000 articles were published describing experiments performed using commercially available systems. The 1038 papers we found represent a $ 10% increase over the past year and demonstrate that the implementation of biosensors continues to expand at a healthy pace. We evaluated the data presented in each paper and compiled a 'top 10' list. These 10 articles, which we recommend every biosensor user reads, describe wellperformed kinetic, equilibrium and qualitative/screening studies, provide comparisons between binding parameters obtained from different biosensor users, as well as from biosensor-and solution-based interaction analyses, and summarize the cutting-edge applications of the technology. We also re-iterate some of the experimental pitfalls that lead to sub-optimal data and over-interpreted results. We are hopeful that the biosensor community, by applying the hints we outline, will obtain data on a par with that presented in the 10 spotlighted articles. This will ensure that the scientific community at large can be confident in the data we report from optical biosensors.

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Redox Potential Regulates Binding of Universal Minicircle Sequence Binding Protein at the Kinetoplast DNA Replication Origin

Cited by 56 publications

References 79 publications

Binding of the Universal Minicircle Sequence Binding Protein at the Kinetoplast DNA Replication Origin

Binding of the Universal Minicircle Sequence Binding Protein at the Kinetoplast DNA Replication Origin

In Search of Trypanocidal Drugs

Survey of the year 2004 commercial optical biosensor literature

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