Unique molecular architecture of silk fibroin in the waxmoth, Galleria mellonella
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
11886872
DOI
10.1074/jbc.m201622200
PII: S0021-9258(19)66859-6
Knihovny.cz E-zdroje
- MeSH
- aminokyselinové motivy MeSH
- DNA metabolismus MeSH
- fibroiny chemie MeSH
- genetická transkripce MeSH
- hedvábí MeSH
- hmyzí proteiny chemie MeSH
- kodon MeSH
- komplementární DNA metabolismus MeSH
- Lepidoptera MeSH
- modely genetické MeSH
- molekulární modely MeSH
- molekulární sekvence - údaje MeSH
- můry MeSH
- northern blotting MeSH
- polymerázová řetězová reakce s reverzní transkripcí MeSH
- RNA metabolismus MeSH
- sekvence aminokyselin MeSH
- sekvence nukleotidů MeSH
- sekvenční analýza DNA MeSH
- sekvenční homologie aminokyselin MeSH
- Southernův blotting MeSH
- terciární struktura proteinů MeSH
- tkáňová distribuce MeSH
- vazba proteinů MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- DNA MeSH
- fibroiny MeSH
- hedvábí MeSH
- hmyzí proteiny MeSH
- kodon MeSH
- komplementární DNA MeSH
- RNA MeSH
Proteins of silk fibers are characterized by reiterations of amino acid repeats. Physical properties of the fiber are determined by the amino acid composition, the complexity of repetitive units, and arrangement of these units into higher order arrays. Except for very short motifs of 6-10 residues, the length of repetitive units and the number of these units concatenated in higher order assemblies vary in all spider and lepidopteran silks analyzed so far. This paper describes an exceptional silk protein represented by the 500-kDa heavy chain fibroin (H-fibroin) of the waxmoth, Galleria mellonella. Its non-repetitive N-terminal (175 residues) and C-terminal (60 residues) parts, the overall gene organization, and the nucleotide sequence around the TATA box show that it is homologous to the H-fibroins of other Lepidoptera. However, over 95% of the protein consists of highly ordered repetitive structures that are unmatched in other species. The repetitive region includes 11 assemblies AB(1)AB(1)AB(1)AB(2)(AB(2))AB(2) of remarkably conserved polypeptide repeats A (63 amino acid residues), B(1) (43 residues), and B(2) (18 residues). The repeats contain a high proportion of Gly (31.6%), Ala (23.8%), Ser (18.1%), and of residues with long hydrophobic side chains (16% for Leu, Ile, and Val combined). The presence of the GLGGLG and SSAASAA(AA) motifs suggests formation of pleated beta-sheets and their stacking into crystallites. Conspicuous conservation of the apolar sequence VIVI followed by DD or ED is interpreted as indicating the importance of hydrophobicity and electrostatic charge in H-fibroin cross-linking. The environment of G. mellonella larvae within bee cultures requires continuous production of silk that must be both strong and elastic. The spectacular arrangement of the repetitive H-fibroin region apparently evolved to meet these requirements.
Citace poskytuje Crossref.org
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GENBANK
AF095239, AF095240