a hypothesis for bacteriophage dna packaging motors噬菌体dna包装汽车的假说.pdfVIP

Viruses 2010, 2, 1821-1843; doi:10.3390/v2091821 OPEN ACCESS viruses ISSN 1999-4915 /journal/viruses Article A Hypothesis for Bacteriophage DNA Packaging Motors Philip Serwer Department of Biochemistry, The University of Texas Health Science Center, San Antonio, Texas 78229-3900, USA; E-Mail: serwer@ Received: 4 June 2010; in revised form: 12 August 2010 / Accepted: 18 August 2010 / Published: 26 August 2010 Abstract: The hypothesis is presented that bacteriophage DNA packaging motors have a cycle comprised of bind/release thermal ratcheting with release-associated DNA pushing via ATP-dependent protein folding. The proposed protein folding occurs in crystallographically observed peptide segments that project into an axial channel of a protein 12-mer (connector) that serves, together with a coaxial ATPase multimer, as the entry portal. The proposed cycle begins when reverse thermal motion causes the connector’s peptide segments to signal the ATPase multimer to bind both ATP and the DNA molecule, thereby producing a dwell phase recently demonstrated by single-molecule procedures. The connector-associated peptide segments activate by transfer of energy from ATP during the dwell. The proposed function of connector/ATPase symmetry mismatches is to reduce thermal noise-induced signaling errors. After a dwell, ATP is cleaved and the DNA molecule released. The activated peptide segments push the releas