The amino acid sequence and stability predictions of the hinge region in myosin subfragment 2.

Lu, Renne Chen; Wong, Anna

doi:10.1016/s0021-9258(19)83643-8

Cited by 41 publications

(10 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…No difference was observed between papain and chymotryptic rod in these experiments. This was expected since the digestion sites for papain and chymotrypsin are only two residues apart in the primary sequence (Lu & Wong, 1985).…”

Section: Methodsmentioning

confidence: 93%

“…The cleavage rate of activated systems was found to be ~100-fold greater than in rigor or relaxed psoas fibers, and these data have been taken to indicate helix melting during the active cross-bridge cycle. Other indications of a lower stability of the "hinge" region have come from analysis of the amino acid sequence of rabbit myosin rod (Lu & Wong, 1985) and rat myosin rod (Strehler et al, 1986). These authors find that a region of amino acids between short S-2 and LMM has significantly lower helix-forming probability than the flanking regions.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Thermal stability of myosin rod from various species

Rodgers¹,

Karr²,

Biedermann³

et al. 1987

Biochemistry

View full text Add to dashboard Cite

The radius of gyration and fraction helix as a function of temperature have been determined for myosin rod from four different species: rabbit, frog, scallop, and antarctic fish. Measurements from sodium dodecyl sulfate gel electrophoresis indicate that all particles have the same molecular weight (approximately 130K). All fragments are nearly 100% alpha-helical at low temperatures (0-5 degrees C). The melting profiles for each are qualitatively similar in shape, but their midpoints are shifted along the temperature axis in the following order: antarctic fish (Tm = 33 degrees C), scallop (Tm = 39 degrees C), frog (Tm = 45 degrees C), and rabbit (Tm = 49 degrees C). Corresponding radius of gyration vs temperature profiles for each species are shifted to lower temperatures (approximately 5-8 degrees C) with respect to the optical rotation melting curves. From plots of radius of gyration vs fraction helix, we find a marked drop in the radius of gyration (from 43 to approximately 34 nm) with less than a 5% decrease in fraction helix for rabbit, frog, and antarctic fish rods, whereas the radius of gyration of scallop rod never exceeds 34 nm. Results indicate hinging of the myosin rod of each species. The thermal stabilities of the myosin rods shift in parallel with the working temperature of their respective muscles.

show abstract

Section: Methodsmentioning

confidence: 93%

Section: Discussionmentioning

confidence: 99%

Thermal stability of myosin rod from various species

Rodgers¹,

Karr²,

Biedermann³

et al. 1987

Biochemistry

View full text Add to dashboard Cite

show abstract

“…Apart from the short, nonhelical, NH2-terminal segment, paramyosin is largely a coiled coil, and by sequence identity, aligns with the COOH-terminal three fourths of the myosin rod, as shown here; the corresponding portion of the MHC rod is in effect the light meromyosin sequences that form the backbone of the thick filament (for review of myosin structure see Squire, 1981). Based on the "hinge" definition of Lu and Wong (1985), the NH2-terminal portion of the MHC rod that is not contained in the shorter paramyosin molecule, the "prehinge region," is part of heavy meromyosin subfragment 2 ($2). (b) Schematic diagram of a longitudinal section of the central region of the bipolar thick filament.…”

mentioning

confidence: 99%

Hydrophobicity variations along the surface of the coiled-coil rod may mediate striated muscle myosin assembly in Caenorhabditis elegans.

Hoppe

Waterston

1996

The Journal of Cell Biology

View full text Add to dashboard Cite

Caenorhabditis elegans body wall muscle contains two isoforms of myosin heavy chain, MHC A and MHC B, that differ in their ability to initiate thick filament assembly. Whereas mutant animals that lack the major isoform, MHC B, have fewer thick filaments, mutant animals that lack the minor isoform, MHC A, contain no normal thick filaments. MHC A, but not MHC B, is present at the center of the bipolar thick filament where initiation of assembly is thought to occur (Miller, D.M.,I. Ortiz, G.C. Berliner, and H.F. Epstein. 1983. Cell. 34:477-490). We mapped the sequences that confer A-specific function by constructing chimeric myosins and testing them in vivo. We have identified two distinct regions of the MHC A rod that are sufficient in chimeric myosins for filament initiation function. Within these regions, MHC A displays a more hydrophobic rod surface, making it more similar to paramyosin, which forms the thick filament core. We propose that these regions play an important role in filament initiation, perhaps mediating close contacts between MHC A and paramyosin in an antiparallel arrangement at the filament center. Furthermore, our analysis revealed that all striated muscle myosins show a characteristic variation in surface hydrophobicity along the length of the rod that may play an important role in driving assembly and determining the stagger at which dimers associate.

show abstract

“…Myosin rods may also play an important role in the regulation of mechanochemical energy transduction. Investigations along these lines have been intensively carried out, especially focusing on the S2 region (Sutoh et al, 1978;Ueno & Harrington, 1984, 1986a; Lu & Wong, 1985;Lovell et al, 1988;Harrington et al, 1990;Sugi et al, 1992). Even given such extensive studies, the exact role of the S2 or hinge region in the rod which is essential to myosin functions and how these regions are regulated Eire not satisfactorily understood.…”

mentioning

confidence: 99%

Differences in the Thermal Stability of Acclimation Temperature-Associated Types of Carp Myosin and Its Rod on Differential Scanning Calorimetry

Nakaya¹,

Watabe²,

Ooi³

1995

Biochemistry

View full text Add to dashboard Cite

Differential scanning calorimetry (DSC) was employed for studying the thermal unfolding of myosin and its rod part prepared from carp acclimated to 10 and 30 degrees C. Differences in the thermal stability reflecting structural properties were clearly demonstrated by the DSC data obtained at pH 8.0 in 0.6 M KCl for the two types of carp myosin and rod. The transition temperatures on myosin and rod given by the major peaks for the 10 degrees C-acclimated carp were 33.9 and 47.4 degrees C and 33.0 and 44.0 degrees C, respectively, assuming two endotherms for this type. Since the shape of the first peaks at 33.9 and 33.0 degrees C was not symmetrical, two peaks having similar transition temperatures overlapped in this temperature range. When the data were analyzed using three endotherms, the three transition temperatures obtained for myosin and rod were 32.8, 34.9, and 47.4 degrees C and 32.9, 33.4, and 44.1 degrees C, respectively. Thus, the position of the first peak for the 10 degrees C-acclimated carp myosin did not change even after removal of the large subfragment-1 part, but the transition of the second peak shifted to a lower temperature by about 3 degrees C. The myosin and rod from carp acclimated to 30 degrees C showed three distinct peaks at 35.9, 39.7, and 49.1 degrees C and 34.5, 39.7, and 46.7 degrees C, respectively. The position of the largest peak for myosin remained unchanged, and the shift of the peak position of the highest temperature was about 3 degrees C, as obtained for the 10 degrees C-acclimated carp.(ABSTRACT TRUNCATED AT 250 WORDS)

show abstract

The amino acid sequence and stability predictions of the hinge region in myosin subfragment 2.

Cited by 41 publications

References 34 publications

Thermal stability of myosin rod from various species

Thermal stability of myosin rod from various species

Hydrophobicity variations along the surface of the coiled-coil rod may mediate striated muscle myosin assembly in Caenorhabditis elegans.

Differences in the Thermal Stability of Acclimation Temperature-Associated Types of Carp Myosin and Its Rod on Differential Scanning Calorimetry

Contact Info

Product

Resources

About