Sequence conservation in the C-terminal region of spider silk proteins (Spidroin) from Nephila clavipes (Tetragnathidae) and Araneus bicentenarius (Araneidae)

J Biol Chem. 1994 Mar 4;269(9):6661-3.

Abstract

The polymerase chain reaction (PCR) has been used to amplify the portion of the Spidroin 1 gene that codes for the C-terminal part of the silk protein of the spider Nephila clavipes. Along with some substitution mutations of minor consequence, the PCR-derived sequence reveals an additional base missing from the previously published Nephila Spidroin 1 sequence. Comparison of the PCR-derived sequence with the equivalent region of Spidroin 2 indicates that the insertion of this single base results in greatly increased similarity in the resulting amino acid sequences of Spidroin 1 and Spidroin 2 (75% over 97 amino acids). The same PCR primers also amplified a fragment of the same length from Araneus bicentenarius. This sequence is also very similar to Spidroin 1 of Nephila (71% over 238 bases excluding the PCR primers, which translates into 76% over 79 amino acids).

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Conserved Sequence*
  • DNA / isolation & purification
  • DNA / metabolism
  • DNA Primers
  • Fibroins*
  • Insect Proteins*
  • Molecular Sequence Data
  • Polymerase Chain Reaction
  • Proteins / chemistry
  • Proteins / genetics*
  • Sequence Homology, Amino Acid
  • Sequence Homology, Nucleic Acid
  • Silk*
  • Spiders / genetics*
  • Spiders / metabolism

Substances

  • DNA Primers
  • Insect Proteins
  • Proteins
  • Silk
  • spidroin 1
  • DNA
  • Fibroins

Associated data

  • GENBANK/U03847
  • GENBANK/U03848