TY - JOUR
T1 - In indirect flight muscles Drosophila projectin has a short PEVK domain, and its NH2-terminus is embedded at the Z-band
AU - Ayme-Southgate, Agnes
AU - Saide, Judith
AU - Southgate, Richard
AU - Bounaix, Christophe
AU - Cammarato, Anthony
AU - Patel, Sunita
AU - Wussler, Catherine
N1 - Funding Information:
We want to thank Drs B. Bullard, and D. Kiehart for providing antibodies against various myofibrillar proteins. The work presented was supported by the National Institutes of Health/BRIN under Grant No. 8-P0RR16461A to AAS.
PY - 2005/12
Y1 - 2005/12
N2 - Insect indirect flight muscles (IFM) contain a third filament system made up of elastic connecting or C-filaments. The giant protein projectin is the main, if not the only, component of these structures. In this study we found that projectin is oriented within the IFM sarcomere with its NH 2-terminus embedded in the Z-bands. We demonstrate that this protein has an elastic region that can be detected by the movement of specific epitopes following stretch. One possible elastic region is the PEVK-like domain located close to the NH2-terminus. The amino acid length of this region is short, and 52% of its residues are P, E, V or K. We propose a model in which projectin extends from the Z-band to the lateral borders of the A-band. The PEVK-like domain and a series of Ig domains spanning the intervening I-band may provide the elastic properties of projectin.
AB - Insect indirect flight muscles (IFM) contain a third filament system made up of elastic connecting or C-filaments. The giant protein projectin is the main, if not the only, component of these structures. In this study we found that projectin is oriented within the IFM sarcomere with its NH 2-terminus embedded in the Z-bands. We demonstrate that this protein has an elastic region that can be detected by the movement of specific epitopes following stretch. One possible elastic region is the PEVK-like domain located close to the NH2-terminus. The amino acid length of this region is short, and 52% of its residues are P, E, V or K. We propose a model in which projectin extends from the Z-band to the lateral borders of the A-band. The PEVK-like domain and a series of Ig domains spanning the intervening I-band may provide the elastic properties of projectin.
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U2 - 10.1007/s10974-005-9031-8
DO - 10.1007/s10974-005-9031-8
M3 - Article
C2 - 16465474
AN - SCOPUS:33745698374
SN - 0142-4319
VL - 26
SP - 467
EP - 477
JO - Journal of Muscle Research and Cell Motility
JF - Journal of Muscle Research and Cell Motility
IS - 6-8
ER -