Abstract
Low temperatures as well as encounters with host phagocytes are two stresses that have been relatively well studied in many species of bacteria. The exoribonuclease polynucleotide phosphorylase (PNPase) has previously been shown to be required by several species of bacteria, including Yersinia, for low-temperature growth. We have shown that PNPase also enhances the ability of Yersinia to withstand the killing activities of murine macrophages. We have gone on to show that PNPase is required for the optimal functioning of Yersinia's type three secretion system (T3SS), an organelle that injects effector proteins directly into host cells. Surprisingly, the PNPase-mediated effect on T3SS activity is independent of PNPase's ribonuclease activity and instead requires only its S1 RNA-binding domain. In stark contrast, the catalytic activity of PNPase is strictly required for enhanced growth at low temperature. Preliminary experiments suggest that the RNA-binding interface of the S1 domain is critical for its T3SS-enhancing activity. Our findings indicate that PNPase plays versatile roles in promoting Yersinia's survival in response to stressful conditions.
| Original language | English (US) |
|---|---|
| Title of host publication | Advances in Experimental Medicine and Biology |
| Publisher | Springer New York |
| Pages | 217-224 |
| Number of pages | 8 |
| Volume | 603 |
| ISBN (Print) | 9780387721231 |
| DOIs | |
| State | Published - 2007 |
Publication series
| Name | Advances in Experimental Medicine and Biology |
|---|---|
| Volume | 603 |
| ISSN (Print) | 00652598 |
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ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Medicine(all)
Cite this
Polynucleotide phosphorylase and the T3SS. / Rosenzweig, Jason A.; Schesser, Kurt.
Advances in Experimental Medicine and Biology. Vol. 603 Springer New York, 2007. p. 217-224 (Advances in Experimental Medicine and Biology; Vol. 603).Research output: Chapter in Book/Report/Conference proceeding › Conference contribution
}
TY - GEN
T1 - Polynucleotide phosphorylase and the T3SS
AU - Rosenzweig, Jason A.
AU - Schesser, Kurt
PY - 2007
Y1 - 2007
N2 - Low temperatures as well as encounters with host phagocytes are two stresses that have been relatively well studied in many species of bacteria. The exoribonuclease polynucleotide phosphorylase (PNPase) has previously been shown to be required by several species of bacteria, including Yersinia, for low-temperature growth. We have shown that PNPase also enhances the ability of Yersinia to withstand the killing activities of murine macrophages. We have gone on to show that PNPase is required for the optimal functioning of Yersinia's type three secretion system (T3SS), an organelle that injects effector proteins directly into host cells. Surprisingly, the PNPase-mediated effect on T3SS activity is independent of PNPase's ribonuclease activity and instead requires only its S1 RNA-binding domain. In stark contrast, the catalytic activity of PNPase is strictly required for enhanced growth at low temperature. Preliminary experiments suggest that the RNA-binding interface of the S1 domain is critical for its T3SS-enhancing activity. Our findings indicate that PNPase plays versatile roles in promoting Yersinia's survival in response to stressful conditions.
AB - Low temperatures as well as encounters with host phagocytes are two stresses that have been relatively well studied in many species of bacteria. The exoribonuclease polynucleotide phosphorylase (PNPase) has previously been shown to be required by several species of bacteria, including Yersinia, for low-temperature growth. We have shown that PNPase also enhances the ability of Yersinia to withstand the killing activities of murine macrophages. We have gone on to show that PNPase is required for the optimal functioning of Yersinia's type three secretion system (T3SS), an organelle that injects effector proteins directly into host cells. Surprisingly, the PNPase-mediated effect on T3SS activity is independent of PNPase's ribonuclease activity and instead requires only its S1 RNA-binding domain. In stark contrast, the catalytic activity of PNPase is strictly required for enhanced growth at low temperature. Preliminary experiments suggest that the RNA-binding interface of the S1 domain is critical for its T3SS-enhancing activity. Our findings indicate that PNPase plays versatile roles in promoting Yersinia's survival in response to stressful conditions.
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U2 - 10.1007/978-0-387-72124-8_19
DO - 10.1007/978-0-387-72124-8_19
M3 - Conference contribution
C2 - 17966418
AN - SCOPUS:84934443045
SN - 9780387721231
VL - 603
T3 - Advances in Experimental Medicine and Biology
SP - 217
EP - 224
BT - Advances in Experimental Medicine and Biology
PB - Springer New York
ER -