Temperature-dependent developmental variation in lobster muscle myosin heavy chain isoforms.

Gene

Center for Science and Technology in Medicine, School of Postgraduate Medicine, Keele University, North Staffordshire Hospital, Thornburrow Road, Hartshill, Stroke-on-Trent ST4 7QB, UK.

Published: October 2003

The temperature- and developmental-regulation of myosin heavy chain (MyHC) expression and primary sequence was investigated in the abdominal musculature of developing Homarus gammarus larvae acclimated to 10, 14 and 19+/-1 degrees C. MyHC loop 1 (ATP binding) and loop 2 (actin binding) regions were sequenced and compared. The deduced amino acid sequence of MyHC loop 1 showed a development-related increase in net charge from +1 to +2 between larval stages 1 and 2, which was not temperature-dependent. In post-settled stage 9 larvae, minor shifts in amino acid sequence occurred at 19 degrees C, and corresponded to a significant up-regulation of fast myosin mRNA expression. However, no temperature-specific loop 1 isoforms were detected. The deduced amino acid sequence of MyHC loop 2 was not affected by temperature, and the net charge remained +4 throughout development. These findings contrast to previous studies using the common carp, in which temperature-specific MyHC isoform genes were expressed in response to disparate thermal regimes. This raises the question as to whether arthropods do not express specific temperature isoforms but instead rely on shifts in fibre type to accommodate alterations in thermal environment.

Download full-text PDF

Source
http://dx.doi.org/10.1016/s0378-1119(03)00745-5DOI Listing

Publication Analysis

Top Keywords

myhc loop
12
amino acid
12
acid sequence
12
myosin heavy
8
heavy chain
8
deduced amino
8
sequence myhc
8
net charge
8
myhc
5
loop
5

Similar Publications

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!