1991
DOI: 10.1016/0014-5793(91)80349-8
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Rabbit skeletal muscle myosin unfolded carboxyl‐terminus and its role in molecular assembly

Abstract: We have cxprcsscd in E. ecUi segments of the rod portion of rabbit skeletal fart muscle myoxin and conrpnrcd physical propertied of two din'crcnt nprcics, LMM-30 and LMM-SOC', LMM-30 consirrs of 263 amino widr including the original C-tcnninus of nryosin heavy rhnin. LMM-30C is colincar with LMM-30, but is devoid of 17 rckiducs a~ the C-terminus. 'W NMR tpcctroscopy indicates that the Gtcmrinus af LMM-30, but not of LMM30C' is unfolded and freely mobile, Furthermore, the prcrcnt results show that the unfolded … Show more

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Cited by 25 publications
(22 citation statements)
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“…Myosin as well as the chymotryptic myosin subfragment 1 (Sl), myosin rod and LMM were prepared as described [ 121. An LMM fragment comprising the carboxy-terminal 30-kDa portion of rabbit fast skeletal muscle LMM was expressed in Escherichio coli and purified as described [14]. The construct was a generous gift by Dr A. Wittinghofer (Max-Planck-Institute for Molecular Physiology, Dortmund, Germany).…”
Section: Generation Of Stable Proteolytic Fragments Of Myomesinmentioning
confidence: 99%
“…Myosin as well as the chymotryptic myosin subfragment 1 (Sl), myosin rod and LMM were prepared as described [ 121. An LMM fragment comprising the carboxy-terminal 30-kDa portion of rabbit fast skeletal muscle LMM was expressed in Escherichio coli and purified as described [14]. The construct was a generous gift by Dr A. Wittinghofer (Max-Planck-Institute for Molecular Physiology, Dortmund, Germany).…”
Section: Generation Of Stable Proteolytic Fragments Of Myomesinmentioning
confidence: 99%
“…In contrast, LMM fragments greater than 75 kDa were insoluble (lane P of Figure 9b). The teprtr.Digests were sampled at the time points indicated and subjected to SDS/PAGE (%gl.Ln using myosin with partially deleted sequences provide further evidence that deletion of a short peptide at the C-terminus significantly increases its solubility in low-ionic-strength buffer [28], decreases aggregation [29] and increases by 50-fold the critical concentration for myosin rod assembly [30]. In sharp contrast, deleting a peptide of similar length at the N-terminus of the rod or LMM has only minor effects [28,30].…”
Section: Solubility Properties Of Lmm Fragmentsmentioning
confidence: 99%
“…For example, mutations in the COOH terminus of Caenorhabditis elegans unc-54 MHC disrupts myosin filament assembly (Dibb et al, 1985) while fusion proteins containing Acanthamoeba myosin II tail sequences with deletions in the last 100 amino acids fail to assemble (Sinard et al, 1990). However, phosphorylation or deletion of part of the nonhelical COOH-terminal tail piece of Acanthamoeba myosin II has little apparent effect on filament formation (Atkinson et al, 1989;Sathyamoorthy et al, 1990;Ganguly et al, 1990) whereas removal of the 17 COOH-terminal amino acids from rabbit skeletal muscle myosin rod disturbs filament assembly especially at high pH values (Maeda et al, 1991).…”
mentioning
confidence: 99%