Primary structure of proteins from the wing cuticle of the migratory locust, Locusta migratoria.
Wing cuticle from pharate adult locusts, Locusta migratoria, contains several prominent proteins which occur as minor components or are completely absent in other cuticular regions. Six of the wing-specific proteins have been purified and their amino acid sequences determined by combined use of mass spectrometry and automated Edman degradation. During the sequence determination very long sequence runs (90-121 residues) were necessary in order to establish the primary structure. All the wing-specific cuticular proteins from locusts contain the repeated short sequence motif -Ala-Ala-Pro-Ala/Val-, which is common for all hitherto sequenced cuticular proteins from pharate locusts. Several of the wing-specific proteins also possess an N-terminal region rich in glycine, tyrosine and leucine, characteristic for many locust cuticular proteins. Two of the analysed proteins have a conserved 61-residue sequence in common with a previously sequenced protein from locust wing cuticle and with two proteins from the pharate cuticle of adult Tenebrio molitor. Possible roles for the various sequence motifs are discussed.
Krogh
T N
TN
Department of Molecular Biology, Odense University, Denmark.
Skou
L
L
Roepstorff
P
P
Andersen
S O
SO
Højrup
P
P
D000595:Amino Acid Sequence; D000818:Animals; D006110:Grasshoppers / Q000737:chemistry*; D008969:Molecular Sequence Data; D011506:Proteins / Q000737:chemistry*; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D014921:Wings, Animal / Q000737:chemistry*
D011506:Proteins