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Science 22 January 1993:
Vol. 259. no. 5094, pp. 522 - 525
DOI: 10.1126/science.8424176
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Articles

Science, Vol 259, Issue 5094, 522-525
Copyright © 1993 by American Association for the Advancement of Science

articles

Regulation by heme of mitochondrial protein transport through a conserved amino acid motif

JT Lathrop and MP Timko

Department of Biology, University of Virginia, Charlottesville 22901.

A conserved motif, termed the heme regulatory motif (HRM), was identified in the presequences of the erythroid delta-aminolevulinate synthase precursors and was shown to be involved in hemin inhibition of transport of these proteins into mouse mitochondria in vitro. When the HRM was inserted into the presequence of the ornithine transcarbamoylase precursor, a normally unregulated mitochondrial protein, it conferred hemin inhibition on the transport of the chimeric protein. The conserved cysteine within the HRM was shown by site-directed mutagenesis to be required for hemin inhibition.


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