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J. Biol. Chem., Vol. 276, Issue 10, 7442-7449, March 9, 2001
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From the The extension of the PEVK segment of the giant
elastic protein titin is a key event in the elastic response of
striated muscle to passive stretch. PEVK behaves mechanically as an
entropic spring and is thought to be a random coil. cDNA sequencing
of human fetal skeletal PEVK reveals a modular motif with tandem
repeats of modules averaging 28 residues and with superrepeats of seven
modules. Conformational studies of bacterially expressed 53-kDa
fragment (TP1) by circular dichroism suggest that this soluble protein contains substantial polyproline II (PPII) type left-handed helices. Urea and thermal titrations cause gradual and reversible decrease in
PPII content. The absence of sharp melting in urea and thermal titrations suggests that there is no long range cooperativity among the
PPII helices. Studies with solid phase and surface plasmon resonance
assays indicate that TP1 interacts with actin and some but not all
cloned nebulin fragments with high affinity. Interestingly, Ca2+/calmodulin and Ca2+/S100
abolish nebulin/PEVK interaction. We suggest that in aqueous solution,
PEVK is an open and flexible chain of relatively stable structural
folds of the polyproline II type. PEVK region of titin may be involved
in interfilament association with thin filaments in a
calcium/calmodulin-sensitive manner. This adhesion may modulate titin
extensibility and elasticity.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF 321609.
Modular Motif, Structural Folds and Affinity Profiles of the
PEVK Segment of Human Fetal Skeletal Muscle Titin*
,¶
Laboratory of Physical Biology, NIAMS,
National Institutes of Health, Bethesda, Maryland 20892 and
§ Department of Chemistry and Biochemistry, University of
Texas, Austin, Texas 78712
*
Preliminary reports of these findings have been presented in
meeting abstracts (G. Gutierrez-Cruz, A. H. Van Heerden, and K. Wang (1997) Biophys. J. 72, 279 (abstr.);
G. Gutierrez-Cruz, A. H. Van Heerden, and K. Wang (1998)
Biophys. J. 74, 349 (abstr.)) at the 41st and
42nd annual meetings of the Biophysical Society. This work was
supported in part by National Institutes of Health Grant AR 45315 (to
K. W.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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