From: Steve Petermann (
Date: Sun Sep 28 2003 - 08:32:44 EDT

  • Next message: Hofmann, Jim: "RE: Reference needed for "Newton's comets""


    Thanks so much for your comments. It just points out that for the
    biolocial/chemical lay person(like me) it is really not possible to evaluate
    the argumentation. The best one can do is look for the integrity and
    scientific honest of the individuals and accept that no firm answer is

    Steve Petermann

    ----- Original Message -----
    From: "Peter Ruest" <>
    To: "Steve Petermann" <>; <>
    Sent: Saturday, September 27, 2003 11:55 PM
    Subject: Re: RFEP & ID

    > > Dave Wrote:
    > > > Where do I find the ID
    > > > research that has forced a reconsideration of "Darwinism"?
    > >
    > > I'm no biologist so a lot in their discussions are over my head but the
    > > threads on flagellum seem particularly good in delineating the ID vs.
    > > Darwinism issues. It's been such a long thread they have two with
    > > pages:
    > >
    > >
    > >
    > >
    > >
    > > For those who are well versed in this field, if they have an opinion on
    > > these threads, I'd appreciate hearing it.
    > >
    > > Steve Petermann
    > Hi, Steve
    > I am not "well versed" in this field, but I am a biochemist and thought
    > you might be interested in this.
    > Here is a copy of a comment about the evolution of the flagellum I
    > posted a year ago to this list:
    > ..................................................................
    > Date: Thu, 24 Oct 2002 06:53:24 +0200
    > From: Peter Ruest <>
    > Subject: Irreducible complexity and the flagellum
    > Some time ago, on this list, Behe's and Dembski's use of the bacterial
    > flagellum as a system of irreducible complexity was dismissed with the
    > claim that it probably evolved out of the type III protein secretion
    > system. I tried to check the evidence available to support this claim.
    > A comprehensive review of the type III system is found in Hueck C.J.,
    > "Type III protein secretion systems in bacterial pathogens of animals
    > and plants", Microbiology and Molecular Biology Reviews 62 (1998),
    > 379-433.
    > The type III system investigated most thoroughly is the one of the pest
    > (or bubonic plague) pathogen Yersinia pestis and two other Yersinia
    > species. There are 10 genes showing some sequence similarity between the
    > Yersinia type III system and flagellar proteins (of Escherichia coli,
    > Salmonella typhimurium, and Bacillus subtilis). All of these flagellar
    > proteins belong to the basal body of the flagellum which is inserted
    > into the cytoplasmic (inner) membrane. According to Hueck's drawing, the
    > basal body of the flagellar system consists of the MS (outer) and C
    > (inner) rings, encased in what I call the bearing, and the ATPase
    > attached on the cytoplasmic side. The basal body constitutes (together
    > with other components) the export system for flagellar constituents and
    > the driving machinery for flagellar rotation. The corresponding Yersinia
    > proteins also belong mostly to the part of the type III system
    > presumably embedded in the cytoplasmic membrane. At least 30 other
    > proteins of the flagellar system, comprising the flagellar hook, the
    > connection (P ring) of the hook to the basal body, the bearing (L ring)
    > of the hook within the outer membrane, and the flagellum proper, have no
    > homologs in the type III system. The Yersinia type III system, as well,
    > comprises at least 25 other proteins having no homologs in the flagellar
    > system. The 10 presumed homologs (or partial homologs) are as follows:
    > Flagellum: Length: Location: Function: Type III: Length: Function:
    > FliF 560 MS ring YscJ 236
    > FliG 331 C ring torque YscD 419
    > FliN 137 C ring YscQ 307
    > FliH 235 bearing 1 YscL 223
    > FliP 245 bearing 2 YscR 217
    > FliQ 89 bearing 3 YscS 88
    > FliR 261 bearing 4 YscT 261
    > FlhB 383 bearing 5 export YscU 354
    > FlhA 692 bearing 6 LcrD 704 export
    > FliI 456 cytoplasm ATPase YscN 439 ATPase
    > The flagellum proteins are those of E.coli or S.typhimurium, the type
    > III system proteins those of Y.pestis, Y.pseudotuberculosis, or
    > Y.enterolytica. The lengths are in amino acid residues. The location of
    > most type III system proteins is unknown, but inferred from that of the
    > flagellar homologs. The functions are usually unknown.
    > Synteny in the genome is restricted to FliP-Q-R with YscR-S-T.
    > The similarities between the FliP-Q-R / YscR-S-T systems and
    > (especially) the FliN-G / YscD-Q systems are weak.
    > In some cases, e.g. FliF / YscJ, the similar proteins are probably
    > unrelated. The FliF-like domain in YscJ may reflect their binding to
    > other components of the export apparatus. Systems III are unlikely to
    > have an MS ring analog, but may form a bridge across the periplasm to
    > the outer membrane.
    > FliI / YscN, which have ATPase activity, show similarities to the alpha
    > and beta subunits of the F1 component of the F0F1 proton translocating
    > ATPases; the most highly conserved regions are two GTP-binding domains
    > and the Mg2+-binding motif around the ATPase-catalytic domain. FliI
    > provides the energy for the export of flagellum units. The similarity
    > between FliI and YscN appears to be due to similar requirements of their
    > common ATPase functions.
    > Thus, the flagellum and the type III export system are two very complex
    > systems composed of a few dozen specific proteins, of which 25-30% show
    > some sequence similarities between the two systems. The 10 similar
    > proteins constitute the majority of the proteins found in all type III
    > export systems, as well as the flagellar basal body, whereas the parts
    > of the type III systems lying outside the cytoplasmic membrane show
    > homologies to different export systems, such as the type II secretion
    > systems and other transport pathways, but not to the flagellar system.
    > Hueck therefore suggests that the type III system may have evolved from
    > a combination of a flagellar basal body and a type II secretion system.
    > Notice that he doesn't propose that the flagellar system arose from a
    > type III export system!
    > In any case, the similarities between flagellum and type III export are
    > very restricted, making any derivation claim highly speculative. Whether
    > the sequence similarities which do exist derive from divergence from
    > common ancestral genes or from functional convergences remains equally
    > uncertain.
    > Does this situation "explain" the flagellum and demonstrate that it is
    > not "irreducibly complex"? I doubt it. The claim remains to be
    > substantiated.
    > Peter
    > ...............................................................
    > --
    > Dr. Peter Ruest, CH-3148 Lanzenhaeusern, Switzerland
    > <> - Biochemistry - Creation and evolution
    > "..the work which God created to evolve it" (Genesis 2:3)

    This archive was generated by hypermail 2.1.4 : Sun Sep 28 2003 - 08:35:47 EDT