Charged flanking residues control the efficiency of membrane insertion of the first transmembrane segment in yeast mitochondrial Mgm1p
2011 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 585, no 8, 1238-1242 p.Article in journal (Refereed) Published
Mgm1p is a nuclearly encoded GTPase important for mitochondrial fusion. Long and short isoforms of the protein are generated in a unique alternative topogenesis process in which the most N-terminal of two hydrophobic segments in the protein is inserted into the inner mitochondrial membrane in about half of the molecules and translocated across the inner membrane in the other half. In the latter population, the second hydrophobic segment is cleaved by the inner membrane protease Pcp1p, generating the short isoform. Here, we show that charged residues in the regions flanking the first segment critically affect the ratio between the two isoforms, providing new insight into the importance of charged residues in the insertion of proteins into the mitochondrial inner membrane.
Place, publisher, year, edition, pages
2011. Vol. 585, no 8, 1238-1242 p.
Mgm1p, Mitochondria, TIM23, Transmembrane helix, Yeast, Saccharomyces cerevisiae
IdentifiersURN: urn:nbn:se:su:diva-68816DOI: 10.1016/j.febslet.2011.03.056ISI: 000289505400021OAI: oai:DiVA.org:su-68816DiVA: diva2:474265
authorCount :42012-01-092012-01-072012-12-12Bibliographically approved