Threonine-77 Is a Determinant of the Low-Temperature Conditioning of the Most Abundant Isoform of Tropomyosin in Atlantic Salmon.

Biochemistry
A Madhushika M SilvaDavid H Heeley

Abstract

The Atlantic salmon Salmo salar survives below 10 °C. The main skeletal muscle is composed of a single isoform of tropomyosin (classified as Tpm1 α-fast) that is >92% identical to the mammalian homologue. How salmon Tpm1 maintains flexibility is investigated by reversing the only full charge substitution; threonine-77(g) in salmon and lysine in other vertebrates. The mutation (Thr-77 to Lys), which falls within a known destabilizing alanine cluster, (i) yields a useful electrophoretic shift in the absence and presence of an anionic detergent, (ii) increases the Tms of both cooperative transitions (calorimetry, 0.1 M salt, pH 7) [35 °C (minor) and 44 °C (major); ΔTm1 = 5 °C, ΔTm2 = 3.5 °C], (iii) increases the Tm of CN1A (residues 11-127) to 53 °C (ΔTm = 13 °C), a value similar to that of mammalian CN1A, (iv) markedly reduces the rate of proteolysis at Leu-169, and (v) weakens the affinity of salmon Tpm1 for troponin-Sepharose. Glu-82(e), the interstrand ionic partner of Lys-77(g), is conserved. The change in ionic interactions at this locus is postulated to be "sensed" in actin period 5 (residues 166-207) and likely beyond. Wild type (acetylated) salmon Tmp1 binds more tightly to F-actin at 4 °C than at 22 °C, which is the oppo...Continue Reading

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