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Receptor sequence in the terminal protein of bacteriophage M2 that interacts with an RGD (Arg-Gly-Asp) sequence of

H Kobayashi1, K Kitabayashi, K Matsumoto

  • 1Life Science Institute, Sophia University, Tokyo, Japan.

Virology
|December 1, 1991
PubMed

Insights

The Arg-Gly-Asp (RGD) sequence in primer proteins is crucial for initiating DNA replication in bacteriophages M2 and phi 29. Researchers identified a homologous sequence (KKIPPDD) in the terminal proteins, suggesting it acts as the RGD receptor.

Area of Science:

  • Molecular Biology
  • Virology
  • Biochemistry

Background:

  • Protein-primed DNA replication is essential for certain bacteriophages, including M2 and phi 29.
  • The Arg-Gly-Asp (RGD) sequence on primer proteins plays a role in recognizing terminal proteins (TP) at replication initiation sites.

Purpose of the Study:

  • To investigate the interaction between primer proteins and terminal proteins (TP) during bacteriophage DNA replication.
  • To identify homologous sequences between bacteriophage TPs and the integrin superfamily.

Main Methods:

  • Sequence comparison of M2 and phi 29 TPs with integrin superfamily members.
  • In vitro experiments using synthetic peptides to assess interference with protein-primed DNA replication and transfection.

Main Results:

  • Identified highly homologous sequences: Lys-Lys-Ile-Pro-Pro-Asp-Asp (KKIPPDD) in M2 and phi 29 TPs and KKGCPPDD in the fibronectin receptor beta-subunit.
  • A synthetic peptide containing KKIPPDD inhibited the RGD peptide's effect on transfection and protein-priming reactions.

Conclusions:

  • The KKIPPDD sequence in M2 TP is proposed to be the receptor for the RGD sequence.
  • This finding sheds light on the molecular mechanisms of protein-primed DNA replication initiation in bacteriophages.

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