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Professor George Rogers was interviewed in 2008 for the Interviews with Australian scientists series. By viewing the interviews in this series, or reading the transcripts and extracts, your students can begin to appreciate Australia's contribution to the growth of scientific knowledge.
The following summary of Roger’s career sets the context for the extract chosen for these teachers notes. The extract highlights Roger’s work on the amino acid composition of the inner root sheath (a part of the hair or wool follicle structure).
George Ernest Rogers was born in Melbourne, Victoria in 1927. He was educated at the University of Melbourne graduating with a BSc (1949) and MSc (1951), in which he investigated the purification of the protein hormone, secretin. Rogers then joined the Biochemistry Unit at the Wool Research Laboratories (WRL) of CSIRO as a research officer. While at the WRL he won a CSIRO scholarship to study the structure and biochemistry of the wool follicle at the University of Cambridge, UK, where he graduated with a PhD in 1956. Rogers returned to Australia and the Division of Protein Chemistry at CSIRO as a senior research officer (1957-62). During this time he developed special techniques for sectioning keratins for viewing under the electron microscope.
Rogers joined the department of biochemistry at the University of Adelaide in 1963 where he began as a reader (1963-77), before being promoted to professor (1978-92). Rogers also served as department head from 1988 to 1992. In 1992 Rogers became an emeritus professor at the University of Adelaide and in 1995 he was asked to be the program manager of Premium Quality Wool CRC (1995-2000). During his career Rogers made key finding in the field of hair research. In particular he looked at the molecular structure of hair keratins and investigated how to manipulate their properties through gene expression and regulation.
Professor Rogers has been honoured throughout his career. Some of his awards include the Lemburg Medal from the Australian Society for Biochemistry and Molecular Biology (1976), a DSc from the University of Adelaide (1976) and the Centenary Medal (2001). Rogers was elected a Fellow of the Australian Academy of Science in 1977.
You became interested in the inner root sheath at about that time, I believe.
That’s true. The wool fibre, like hair fibres generally, grows up out of a follicle, and it has a surround of another cellular layer called the inner root sheath. This undergoes a differentiation process that resembles the hair cortex itself but, as I found out, is chemically widely different. Nothing really was known about the chemistry of that layer, but when I’d done some preliminary work on it, using histochemistry, it gave reactions which were markedly different from those of keratin. So I suspected there was something significant there, but I had to delve into it using some biochemical techniques.
In order to do that, I realised, after removing the follicle by plucking it out of the skin one could actually micro-dissect off the sheath – it would come away quite easily – under a dissecting microscope. But analytical techniques then were not what they are today, so it was a quantitative business, and I had to get enough material. The follicles in the sheep skin were too small to be dissected like that, and I had to go to something bigger. I had thought about getting seal whiskers or something like that, but in the end I used rats. I used the snout as it has large whiskers, vibrissae and follicles. I was able to obtain about 100 rats and dissected some hundreds of follicles to get enough of the inner root sheath. [laugh] I intended to clean up the tissue and then just hydrolyse it to obtain the amino acid composition; the cells fill up solidly with protein, in the same way as the fibre fills up with keratin. Our protein chemistry colleagues said, however, ‘Oh, you’re wasting your time; it’s going to be like keratin’. In those days we knew very little about amino acid sequences of complex proteins like keratin.
I was delighted by the first qualitative analysis. It was done by the old method of paper chromatography, and, lo and behold, there was a pattern of spots of amino acids distributed on this twodimensional chromatogram that were different in intensity from what you see if you hydrolyse keratin and separate its amino acids. And there was a spot which was not in keratin. That was a moment for jubilation. I was able to show my protein chemistry colleagues that they were not right.
Then that strange spot was finally identified. I took a lot of pains to make sure the identification was correct, and it turned out to be the amino acid citrulline, which is related to arginine. There had not been any substantiated identification of citrulline in proteins. Arginine has a so-called guanidino side chain, which is basic, whereas citrulline has an ureido, urea-type side chain, which is not basic but neutral. The worry was that there might be some peculiar linkage between citrulline and a protein that was perhaps not covalent, but it proved to be definitely covalently linked.
So, where did it come from? In the late 1950s it was not known how proteins were synthesised. Although transfer RNA, which is one of the intermediates in the protein synthesis sequence, was known, the actual mechanism hadn’t been worked out; we didn’t know anything about the code at that time. There were all sorts of lateral thinking as to what might be going on. I will discuss that a little later.
Talking about wool proteins reminds me that Ian O’Donnell, when he dissolved up a seagull feather or emu feather, found only one protein, whereas the work done in your laboratory on the chick feather found dozens of proteins. How do you explain that?
The simplest explanation is that there is a family of genes and they are closely linked; they appear to have arisen, back in evolutionary history, through gene duplication. There are several tens of different genes, maybe 50, but the encoding DNA sequences differ only slightly. There have been mutations between these members so that in total properties, in terms of protein isolation and characterisation, you can’t separate them; they behave very much the same. So, with his techniques at the time, he couldn’t show the difference. He could now with techniques like mass spectrometry, I suppose. But we were able to show that there are many genes encoding these families, and that was a major finding at that time.
Select activities that are most appropriate for your lesson plan or add your own. You can also encourage students to identify key issues in the preceding extract and devise their own questions or topics for discussion.
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