scholarly journals Two missense alleles of the Drosophila melanogaster act88F actin gene are strongly antimorphic but only weakly induce synthesis of heat shock proteins.

1987 ◽  
Vol 7 (9) ◽  
pp. 3084-3091 ◽  
Author(s):  
C C Karlik ◽  
D L Saville ◽  
E A Fyrberg
Keyword(s):  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Flight Muscle ◽  
Structure And Function ◽  
Actin Gene ◽  
Wild Type ◽  
Diploid Complement ◽  
Flight Muscles ◽  
Shock Proteins ◽  
And Function

We have characterized two extant mutations of the flight muscle-specific act88F actin gene of Drosophila melanogaster. Both defective alleles were recovered from flightless mutants isolated previously (K. Mogami and Y. Hotta, Mol. Gen. Genet. 183:409-417, 1981). By directly sequencing the mutant alleles, we demonstrated that in act88FIfm(3)2 a single G-C to A-T transition converted arginine-28 to cysteine and that in act88FIfm(3)4 a single A-T to T-A transversion changed isoleucine-76 to phenylalanine. We showed that the actins encoded by either allele were strongly antimorphic. Mutant alleles effectively disrupted myofibril structure and function in the flight muscles of strains having the diploid complement of wild-type act88F genes. However, unlike antimorphic actins encoded by three previously characterized act88F alleles, neither that encoded by act88FIfm(3)2 nor that encoded by act88FIfm(3)4 was a strong inducer of heat shock protein synthesis.

Two missense alleles of the Drosophila melanogaster act88F actin gene are strongly antimorphic but only weakly induce synthesis of heat shock proteins

1987 ◽  
Vol 7 (9) ◽  
pp. 3084-3091
Author(s):  
C C Karlik ◽  
D L Saville ◽  
E A Fyrberg
Keyword(s):  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Flight Muscle ◽  
Structure And Function ◽  
Actin Gene ◽  
Wild Type ◽  
Diploid Complement ◽  
Flight Muscles ◽  
Shock Proteins ◽  
And Function

We have characterized two extant mutations of the flight muscle-specific act88F actin gene of Drosophila melanogaster. Both defective alleles were recovered from flightless mutants isolated previously (K. Mogami and Y. Hotta, Mol. Gen. Genet. 183:409-417, 1981). By directly sequencing the mutant alleles, we demonstrated that in act88FIfm(3)2 a single G-C to A-T transition converted arginine-28 to cysteine and that in act88FIfm(3)4 a single A-T to T-A transversion changed isoleucine-76 to phenylalanine. We showed that the actins encoded by either allele were strongly antimorphic. Mutant alleles effectively disrupted myofibril structure and function in the flight muscles of strains having the diploid complement of wild-type act88F genes. However, unlike antimorphic actins encoded by three previously characterized act88F alleles, neither that encoded by act88FIfm(3)2 nor that encoded by act88FIfm(3)4 was a strong inducer of heat shock protein synthesis.

scholarly journals Alterations in flight muscle ultrastructure and function in Drosophila tropomyosin mutants.

1996 ◽  
Vol 135 (3) ◽  
pp. 673-687 ◽  
Author(s):  
A J Kreuz ◽  
A Simcox ◽  
D Maughan
Keyword(s):  
Amino Acid ◽  
Power Output ◽  
Flight Muscle ◽  
Structure And Function ◽  
Wild Type ◽  
Muscle Tropomyosin ◽  
Ultrastructure And Function ◽  
And Function ◽  
Net Power Output ◽  
Current Report

Drosophila indirect flight muscle (IFM) contains two different types of tropomyosin: a standard 284-amino acid muscle tropomyosin, Ifm-TmI, encoded by the TmI gene, and two > 400 amino acid tropomyosins, TnH-33 and TnH-34, encoded by TmII. The two IFM-specific TnH isoforms are unique tropomyosins with a COOH-terminal extension of approximately 200 residues which is hydrophobic and rich in prolines. Previous analysis of a hypomorphic TmI mutant, Ifm(3)3, demonstrated that Ifm-TmI is necessary for proper myofibrillar assembly, but no null TmI mutant or TmII mutant which affects the TnH isoforms have been reported. In the current report, we show that four flightless mutants (Warmke et al., 1989) are alleles of TmI, and characterize a deficiency which deletes both TmI and TmII. We find that haploidy of TmI causes myofibrillar disruptions and flightless behavior, but that haploidy of TmII causes neither. Single fiber mechanics demonstrates that power output is much lower in the TmI haploid line (32% of wild-type) than in the TmII haploid line (73% of wild-type). In myofibers nearly depleted of Ifm-TmI, net power output is virtually abolished (< 1% of wild-type) despite the presence of an organized fibrillar core (approximately 20% of wild-type). The results suggest Ifm-TmI (the standard tropomyosin) plays a key role in fiber structure, power production, and flight, with reduced Ifm-TmI expression producing corresponding changes of IFM structure and function. In contrast, reduced expression of the TnH isoforms has an unexpectedly mild effect on IFM structure and function.

scholarly journals Structure and Function of Small Heat Shock Proteins from the Magnetotactic Bacterium Magnetospirillum magneticum AMB-1

2010 ◽  
Vol 67 (12) ◽  
pp. 698-704 ◽  
Author(s):  
Tetsuya ABE ◽  
Shinpei ITO ◽  
Naoya NISHI ◽  
Yoshihiro TSUKADA ◽  
Takuo YASUNAGA ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Heat Shock Proteins ◽  
Structure And Function ◽  
Magnetotactic Bacterium ◽  
Shock Proteins ◽  
And Function ◽  
Magnetospirillum Magneticum

scholarly journals Evolution, structure and function of the small heat shock proteins in plants

1996 ◽  
Vol 47 (3) ◽  
pp. 325-338 ◽  
Author(s):  
Elizabeth R. Waters ◽  
Garrett J. Lee ◽  
Elizabeth Vierling
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Heat Shock Proteins ◽  
Structure And Function ◽  
Shock Proteins ◽  
And Function

Some like it hot: the structure and function of small heat-shock proteins

2005 ◽  
Vol 12 (10) ◽  
pp. 842-846 ◽  
Author(s):  
Martin Haslbeck ◽  
Titus Franzmann ◽  
Daniel Weinfurtner ◽  
Johannes Buchner
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Heat Shock Proteins ◽  
Structure And Function ◽  
Shock Proteins ◽  
And Function

scholarly journals Structure and Function: Heat Shock Proteins and Adaptive Immunity

2007 ◽  
Vol 179 (4) ◽  
pp. 2035-2040 ◽  
Author(s):  
Babak Javid ◽  
Paul A. MacAry ◽  
Paul J. Lehner
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Adaptive Immunity ◽  
Structure And Function ◽  
Shock Proteins ◽  
And Function

A genetic deficiency that spans the flightin gene of Drosophila melanogaster affects the ultrastructure and function of the flight muscles.

1998 ◽  
Vol 201 (13) ◽  
pp. 2033-2044 ◽  
Author(s):  
J O Vigoreaux ◽  
C Hernandez ◽  
J Moore ◽  
G Ayer ◽  
D Maughan
Keyword(s):  
Drosophila Melanogaster ◽  
Flight Muscle ◽  
Mechanical Analysis ◽  
Genetic Deficiency ◽  
Intact Core ◽  
Flight Muscles ◽  
Ultrastructure And Function ◽  
And Function ◽  
Net Power Output

We have developed a reverse-genetic approach to study the function of flightin, a unique protein of the flight muscle myofibril of Drosophila melanogaster. We describe the generation and characterization of Df(3L)fln1, a lethal genetic deficiency in the 76BE region of the third chromosome which deletes several genes, including the gene for flightin. We show that heterozygous flies harboring the Df(3L)fln1 mutation exhibit both impaired flight and ultrastructural defects in their flight muscle myofibrils. We found that the mutation does not interfere with assembly of the myofibril but leads to disorganization of peripheral myofilaments in adult myofibrils. Most myofibrils, nevertheless, retain an intact core that represents approximately 80 % of the normal lattice diameter. Mechanical analysis of single skinned flight muscle fibers demonstrates that the mutation has no significant effect on net power output but increases the frequency at which maximum power is delivered to the wings, potentially reducing the overall performance of the flight system. The results suggest that flightin is an indispensable part of the flight muscle contractile mechanism.

scholarly journals MUTATIONAL ANALYSIS OF THE REGION SURROUNDING THE 93D HEAT SHOCK LOCUS OF DROSOPHILA MELANOGASTER

Genetics ◽  
1984 ◽  
Vol 106 (2) ◽  
pp. 249-265
Author(s):  
Jym Mohler ◽  
Mary Lou Pardue
Keyword(s):  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Mutational Analysis ◽  
Point Mutations ◽  
Γ Irradiation ◽  
Lethal Mutations ◽  
Complementation Groups ◽  
In Trans ◽  
Shock Locus ◽  
Shock Proteins

ABSTRACT The region containing subdivisions 93C, 93D and 93E on chromosome 3 of Drosophila melanogaster has been screened for visible and lethal mutations. Treatment with three mutagens, γ irradiation, ethyl methanesulfonate and diepoxybutane, has produced mutations that fall into 20 complementation groups, including the previously identified ebony locus. No point mutations affecting the heat shock locus in 93D were detected; however, a pair of deficiencies that overlap in the region of this locus was isolated. Flies heterozygous in trans for this pair of deficiencies are capable of producing all of the major heat shock puffs (except 93D) and the major heat shock proteins. In addition, these flies show recovery of normal protein synthesis following a heat shock.

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