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Characterization, localization, and seasonal changes of the sucrose transporter FeSUT1 in the phloem of Fraxinus excelsior.

Öner-Sieben S, Rappl C, Sauer N, Stadler R, Lohaus G - J. Exp. Bot. (2015)

Bottom Line: The localization and expression pattern point towards functions of FeSUT1 in phloem loading of sucrose as well as in sucrose retrieval.The elevated expression level of FeSUT1 indicated an increased apoplastic carbon export activity from the leaves during spring and late autumn.It is hypothesized that the importance of apoplastic loading is high under low-sucrose conditions and that the availability of two different phloem-loading mechanisms confers advantages for temperate woody species like F. excelsior.

View Article: PubMed Central - PubMed

Affiliation: Molekulare Pflanzenforschung/Pflanzenbiochemie (Botanik), Bergische Universität Wuppertal, Gaußstraße 20, D-42119 Wuppertal, Germany.

No MeSH data available.


Related in: MedlinePlus

Western blot analysis of anti-FeSUT1 antiserum on isolated crude membrane protein extracts from yeast cells expressing FeSUT1 in sense (lane +) and in antisense direction (lane −). (A) Successful blotting was verified by Ponceau S staining. (B) The anti-FeSUT1-antiserum showed a strong specific band at 43kDa on membrane protein extracts from transgenic yeast that expressed FeSUT1 (lane +). The negative control showed no reactions (lane −). (This figure is available in colour at JXB online.)
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Figure 2: Western blot analysis of anti-FeSUT1 antiserum on isolated crude membrane protein extracts from yeast cells expressing FeSUT1 in sense (lane +) and in antisense direction (lane −). (A) Successful blotting was verified by Ponceau S staining. (B) The anti-FeSUT1-antiserum showed a strong specific band at 43kDa on membrane protein extracts from transgenic yeast that expressed FeSUT1 (lane +). The negative control showed no reactions (lane −). (This figure is available in colour at JXB online.)

Mentions: Three polyclonal antisera against a part of the central loop of FeSUT1 were raised in rabbits. The specificity of the antisera was confirmed by western blot analyses using plasma membrane proteins from FeSUT1-expressing yeast cells. All three anti-FeSUT1-antisera resulted in similar signals, but the antiserum of rabbit 1 showed the strongest reaction. It recognized a polypeptide with an apparent molecular weight of 43kDa (FeSUT1 in sense direction, FeSUT1+ in Fig. 2B). No bands were present in the negative control (FeSUT1 in antisense direction, FeSUT1− in Fig. 2B) although similar protein amounts were blotted (Fig. 2A). The apparent molecular weight (43kDa) was lower than the calculated molecular weight (54.2kDa) of FeSUT1, which was also shown for other lipophilic membrane proteins (Beyreuther et al., 1980; Sauer and Tanner, 1984).


Characterization, localization, and seasonal changes of the sucrose transporter FeSUT1 in the phloem of Fraxinus excelsior.

Öner-Sieben S, Rappl C, Sauer N, Stadler R, Lohaus G - J. Exp. Bot. (2015)

Western blot analysis of anti-FeSUT1 antiserum on isolated crude membrane protein extracts from yeast cells expressing FeSUT1 in sense (lane +) and in antisense direction (lane −). (A) Successful blotting was verified by Ponceau S staining. (B) The anti-FeSUT1-antiserum showed a strong specific band at 43kDa on membrane protein extracts from transgenic yeast that expressed FeSUT1 (lane +). The negative control showed no reactions (lane −). (This figure is available in colour at JXB online.)
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC4507781&req=5

Figure 2: Western blot analysis of anti-FeSUT1 antiserum on isolated crude membrane protein extracts from yeast cells expressing FeSUT1 in sense (lane +) and in antisense direction (lane −). (A) Successful blotting was verified by Ponceau S staining. (B) The anti-FeSUT1-antiserum showed a strong specific band at 43kDa on membrane protein extracts from transgenic yeast that expressed FeSUT1 (lane +). The negative control showed no reactions (lane −). (This figure is available in colour at JXB online.)
Mentions: Three polyclonal antisera against a part of the central loop of FeSUT1 were raised in rabbits. The specificity of the antisera was confirmed by western blot analyses using plasma membrane proteins from FeSUT1-expressing yeast cells. All three anti-FeSUT1-antisera resulted in similar signals, but the antiserum of rabbit 1 showed the strongest reaction. It recognized a polypeptide with an apparent molecular weight of 43kDa (FeSUT1 in sense direction, FeSUT1+ in Fig. 2B). No bands were present in the negative control (FeSUT1 in antisense direction, FeSUT1− in Fig. 2B) although similar protein amounts were blotted (Fig. 2A). The apparent molecular weight (43kDa) was lower than the calculated molecular weight (54.2kDa) of FeSUT1, which was also shown for other lipophilic membrane proteins (Beyreuther et al., 1980; Sauer and Tanner, 1984).

Bottom Line: The localization and expression pattern point towards functions of FeSUT1 in phloem loading of sucrose as well as in sucrose retrieval.The elevated expression level of FeSUT1 indicated an increased apoplastic carbon export activity from the leaves during spring and late autumn.It is hypothesized that the importance of apoplastic loading is high under low-sucrose conditions and that the availability of two different phloem-loading mechanisms confers advantages for temperate woody species like F. excelsior.

View Article: PubMed Central - PubMed

Affiliation: Molekulare Pflanzenforschung/Pflanzenbiochemie (Botanik), Bergische Universität Wuppertal, Gaußstraße 20, D-42119 Wuppertal, Germany.

No MeSH data available.


Related in: MedlinePlus