Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 1015-1020 |
| Seitenumfang | 6 |
| Fachzeitschrift | The plant journal |
| Jahrgang | 7 |
| Ausgabenummer | 6 |
| Publikationsstatus | Veröffentlicht - Juni 1995 |
| Extern publiziert | Ja |
Abstract
The mitochondrial ADP/ATP translocator, also called adenine nucleotide translocase (ANT), is synthesized in plants with an N‐terminal extension which is cleaved upon import into mitochondria. In contrast, the homologous proteins of mammals or fungi do not contain such a transient amino terminal presequence. To investigate whether the N‐terminal extension is needed for correct intracellular sorting in vivo, translational fusions were constructed of the translocator cDNA—with and without presequence—with the β‐glucuronidase (gus) reporter gene. The distribution of reporter enzymatic activity in the subcellular compartments of transgenic plants and transformed yeast cells was subsequently analysed. The results show that: (i) the plant translocator presequence is not necessary for the correct localization of the ANT to the mitochondria; (ii) the mitochondrial targeting information contained in the mature part of the protein is sufficient to overcome, to some extent, the presence of plastid transit peptides; and (iii) the presequence alone is not able to target a passenger protein to mitochondria in vivo.
ASJC Scopus Sachgebiete
- Biochemie, Genetik und Molekularbiologie (insg.)
- Genetik
- Agrar- und Biowissenschaften (insg.)
- Pflanzenkunde
- Biochemie, Genetik und Molekularbiologie (insg.)
- Zellbiologie
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in: The plant journal, Jahrgang 7, Nr. 6, 06.1995, S. 1015-1020.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - The N‐terminal extension of the ADP/ATP translocator is not involved in targeting to plant mitochondria in vivo
AU - Mozo, Teresa
AU - Fischer, Karsten
AU - Flügge, Ulf Ingo
AU - Schmitz, Udo
PY - 1995/6
Y1 - 1995/6
N2 - The mitochondrial ADP/ATP translocator, also called adenine nucleotide translocase (ANT), is synthesized in plants with an N‐terminal extension which is cleaved upon import into mitochondria. In contrast, the homologous proteins of mammals or fungi do not contain such a transient amino terminal presequence. To investigate whether the N‐terminal extension is needed for correct intracellular sorting in vivo, translational fusions were constructed of the translocator cDNA—with and without presequence—with the β‐glucuronidase (gus) reporter gene. The distribution of reporter enzymatic activity in the subcellular compartments of transgenic plants and transformed yeast cells was subsequently analysed. The results show that: (i) the plant translocator presequence is not necessary for the correct localization of the ANT to the mitochondria; (ii) the mitochondrial targeting information contained in the mature part of the protein is sufficient to overcome, to some extent, the presence of plastid transit peptides; and (iii) the presequence alone is not able to target a passenger protein to mitochondria in vivo.
AB - The mitochondrial ADP/ATP translocator, also called adenine nucleotide translocase (ANT), is synthesized in plants with an N‐terminal extension which is cleaved upon import into mitochondria. In contrast, the homologous proteins of mammals or fungi do not contain such a transient amino terminal presequence. To investigate whether the N‐terminal extension is needed for correct intracellular sorting in vivo, translational fusions were constructed of the translocator cDNA—with and without presequence—with the β‐glucuronidase (gus) reporter gene. The distribution of reporter enzymatic activity in the subcellular compartments of transgenic plants and transformed yeast cells was subsequently analysed. The results show that: (i) the plant translocator presequence is not necessary for the correct localization of the ANT to the mitochondria; (ii) the mitochondrial targeting information contained in the mature part of the protein is sufficient to overcome, to some extent, the presence of plastid transit peptides; and (iii) the presequence alone is not able to target a passenger protein to mitochondria in vivo.
UR - http://www.scopus.com/inward/record.url?scp=0029311313&partnerID=8YFLogxK
U2 - 10.1046/j.1365-313X.1995.07061015.x
DO - 10.1046/j.1365-313X.1995.07061015.x
M3 - Article
C2 - 7599644
AN - SCOPUS:0029311313
VL - 7
SP - 1015
EP - 1020
JO - The plant journal
JF - The plant journal
SN - 0960-7412
IS - 6
ER -