By Karl Esser, Ulrich Lüttge, Wolfram Beyschlag, Jin Murata
With one quantity every year, this sequence retains scientists and complex scholars trained of the newest advancements and leads to all components of the plant sciences.The current quantity comprises reports on genetics, mobilephone biology, body structure, comparative morphology, systematics, ecology, and crops technology.
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Additional info for Progress in Botany, Vol. 67
The 13-kDa protein represents a prominent mitochondrially encoded protein, which confers sensitivity to the T-toxin. The T-toxin produced by the T race of Cochliobolus heterostrophus, causing the southern corn leaf blight, interacts with the protein, which is located in the inner mitochondrial membrane in an oligomeric arrangement. This induces the formation of a pore that makes the membrane leaky (Dewey et al. 1987; Korth et al. 1991). The binding of the pathotoxin renders the mitochondria incapable of performing oxidative phosphorylation (Kaspi and Siedow 1993; Rhoads et al.
1994; Horn et al. 1996) which represents the only difference between the in organello translation products of fertile and male-sterile lines (Horn et al. 1991). The 16-kDa protein is membrane-bound (Horn et al. 1996) and its expression is specifically reduced in the anthers of fertility restored hybrids (Monéger et al. 1994). The 16-kDa protein seems to be involved in initiating premature programmed cell death in tapetum cells via release of cytochrome C by the mitochondria (Balk and Leaver 2001).
1986b) investigated the in organello translation products of a number of CMS systems. For CMS Milo, they identified an additional 65 kDa protein, for CMS 9E an additional 42 kDa protein and the absence of a 38 kDa protein (Dixon and Leaver 1981). For CMS IS II2 and MS M35-1(B), additional proteins of 12 kDa and 82 kDa, respectively, were detected (Bailey-Serres et al. 1986b). In petunia, Nivison and Hanson (1989) identified the gene product of the CMS-associated pcf gene by using antibodies produced against a synthetic oligopeptide.
Progress in Botany, Vol. 67 by Karl Esser, Ulrich Lüttge, Wolfram Beyschlag, Jin Murata