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• W2023092858 abstract "We have identified a new, double-strand-dependent, mtDNA-binding protein in chick embryo flbroblast (CEF) mitochondria (and inner-membrane-matrix preparations) which demonstrates both an exclusive specific affinity for the displacement loop (D-loop) control region of chick mtDNA and intramitochondrial levels that reflect corresponding changes in mtDNA replication activity both in vivo and in vitro. This ~36 kDa protein (designated aMDP1, avian mitochondrial DNA-binding protein 1) was identified by elution and renaturation following SDS-polyacrylamide gel electrophoresis and by direct isolation from specific mtDNA-protein complexes excised from mobility shift gels. Analysis of the entire 16.7-kb mt genome determined that aMDP1 mediates cleavage of chick mtDNA in vitro at three H- and two L-strand sequence-specific target sites located within a 90-bp A+T-rich genomic tract, theoretically capable of forming stable secondary structures, ~200 bases upstream from the H-strand origin (OH) of replication. Furthermore, gel-isolated aMDP1 relaxes supercoiled mtDNA, and exogenous addition of the protein, in a permeabilized in vitro system, preferentially stimulates the synthesis of H-strand sequences which hybridize to OH-containing fragments. Oncogenic transformation of CEF by Rous sarcoma viruses results in a threefold elevated level of aMDP1, directly correlating with a similarly increased level of mtDNA replication in vivo. Heterologous chick-human crosscompetition experiments showed that aMDP1 also selectively interacts with human (HeLa) D-loop region mtDNA, possibly reflective of an evolutionary importance for aMDP1 interaction in the region. Functionally, we hypothesize that aMDP1 may operate in conjunction with other mtDNA-binding proteins, important in replication and transcription, by potentiating duplex unwinding either prior to or during an initial stage of H-strand synthesis. Together, these results suggest that aMDP1 is a good potential candidate for a nucleus-encoded regulatory protein which communicates with the mt genome during the replication process." @default.
• W2023092858 created "2016-06-24" @default.
• W2023092858 creator A5043255580 @default.
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• W2023092858 date "1992-04-01" @default.
• W2023092858 modified "2023-10-18" @default.
• W2023092858 title "A new chick mitochondrial DNA-binding protein exhibits sequence-specific interaction near heavy-strand replication origin: Cleavage activity, stimulation of mtDNA synthesis, and enhancement in transformed fibroblasts" @default.
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• W2023092858 doi "https://doi.org/10.1016/0014-4827(92)90424-7" @default.
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