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Hot Proteins May Sharpen DNA Tests; Help Bioprocessing

Date:
June 24, 2003
Source:
University Of Maryland Biotechnology Institute
Summary:
Unique heat shock proteins that protect bacteria in undersea hot vents could be used to improve the sensitivity of PCR, the common technique used to amplify bits of DNA for medical and forensic sciences, say researchers with the University of Maryland Biotechnology Institute (UMBI).

WASHINGTON, D.C., BIO2003- Unique heat shock proteins that protect bacteria in undersea hot vents could be used to improve the sensitivity of PCR, the common technique used to amplify bits of DNA for medical and forensic sciences, say researchers with the University of Maryland Biotechnology Institute (UMBI).

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In addition, commercial manufacturing of vaccines, antibiotics and other medically important proteins could become more efficient by incorporating the unique heat shock proteins into microbial cells in those processes. Future use of the proteins could also impact agriculture, fish production and other commercially important biological processes.

Microorganisms that live in deep ocean vents where water exceeds the normal boiling point possess a phenomenal capacity for resisting heat damage." says Frank Robb of UMBI's Center of Marine Biotechnology. When temperatures rise above 103 ' C, they form heat shock proteins that work as chaperones of key proteins in the cell, protecting and allowing them to remain intact at very high temperatures.

Similar chaperone proteins appear in all branches of life. In humans they help prevent cataracts by keeping the proteins in the eye lens fluids from deteriorating. The polymerase chain reaction, or PCR, which is commonly used in clinical medicine, forensic science, evolutionary biology and archeology, and genetic disease diagnostics, relies on a heat stable DNA polymerase.

Robb explains recent experiments at COMB, "We have been able to show that by adding a small heat shock protein from Pyrococcus furiosus to the DNA polymerase enzymes used in the PCR test, you can increase the sensitivity by about ten times.

In addition, when we put the gene encoding these unique chaperone proteins into E. coli, a common bacterium, the resulting genetically modified E. coli strain could grow and survive at higher temperatures," says Robb.

This work is published in: Laksanalamai P, Jiemjit A, Bu Z, Maeder L, Robb FT. (2003) Multi-subunit assembly of the Pyrococcus furiosus small heat shock protein is essential for cellular protection at high temperature. Extremophiles, 7:79-83.

UMBI has patented the small heat shock proteins from P. furiosus. For information on licensing technology, please contact Claude Nash, Vice President Business Development at nash@umbi.umd.edu or 410-385-6328.

The University of Maryland Biotechnology Institute was mandated by the state of Maryland legislature in 1985 as "a new paradigm of state economic development in biotech-related sciences." With five major research and education centers across Maryland, UMBI is dedicated to advancing the frontiers of biotechnology. The centers are the Center for Advanced Research in Biotechnology in Rockville; Center for Biosystems Research in College Park; and Center of Marine Biotechnology, Medical Biotechnology Center, and the Institute of Human Virology, all in Baltimore.


Story Source:

The above story is based on materials provided by University Of Maryland Biotechnology Institute. Note: Materials may be edited for content and length.


Cite This Page:

University Of Maryland Biotechnology Institute. "Hot Proteins May Sharpen DNA Tests; Help Bioprocessing." ScienceDaily. ScienceDaily, 24 June 2003. <www.sciencedaily.com/releases/2003/06/030624090149.htm>.
University Of Maryland Biotechnology Institute. (2003, June 24). Hot Proteins May Sharpen DNA Tests; Help Bioprocessing. ScienceDaily. Retrieved March 28, 2015 from www.sciencedaily.com/releases/2003/06/030624090149.htm
University Of Maryland Biotechnology Institute. "Hot Proteins May Sharpen DNA Tests; Help Bioprocessing." ScienceDaily. www.sciencedaily.com/releases/2003/06/030624090149.htm (accessed March 28, 2015).

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