Allosteric transitions direct protein tagging by PafA, the prokaryotic ubiquitin-like protein (Pup) ligase

Naomi Ofer; Nadav Forer; Maayan Korman; Marina Vishkautzan; Isam Khalaila; Eyal Gur

doi:10.1074/jbc.M112.435842

Allosteric transitions direct protein tagging by PafA, the prokaryotic ubiquitin-like protein (Pup) ligase

Naomi Ofer, Nadav Forer, Maayan Korman, Marina Vishkautzan, Isam Khalaila, Eyal Gur

Ben-Gurion University of the Negev

Research output: Contribution to journal › Article › peer-review

Abstract

Background: The interaction of PafA, the prokaryotic ubiquitin-like ligase, with its protein substrates is poorly understood. Results: Measurements of PafA kinetics reveal cooperative substrate binding and experiments with engineered substrates suggest that PafA forms dimers. Conclusion: The PafA enzymatic mechanism involves allosteric transitions. Significance: PafA interaction with its target substrates is regulated at the enzyme level.

Original language	American English
Pages (from-to)	11287-11293
Number of pages	7
Journal	Journal of Biological Chemistry
Volume	288
Issue number	16
DOIs	https://doi.org/10.1074/jbc.M112.435842
State	Published - 19 Apr 2013

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology
Cell Biology

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abstract = "Background: The interaction of PafA, the prokaryotic ubiquitin-like ligase, with its protein substrates is poorly understood. Results: Measurements of PafA kinetics reveal cooperative substrate binding and experiments with engineered substrates suggest that PafA forms dimers. Conclusion: The PafA enzymatic mechanism involves allosteric transitions. Significance: PafA interaction with its target substrates is regulated at the enzyme level.",

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AU - Ofer, Naomi

AU - Forer, Nadav

AU - Korman, Maayan

AU - Vishkautzan, Marina

AU - Khalaila, Isam

AU - Gur, Eyal

PY - 2013/4/19

Y1 - 2013/4/19

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AB - Background: The interaction of PafA, the prokaryotic ubiquitin-like ligase, with its protein substrates is poorly understood. Results: Measurements of PafA kinetics reveal cooperative substrate binding and experiments with engineered substrates suggest that PafA forms dimers. Conclusion: The PafA enzymatic mechanism involves allosteric transitions. Significance: PafA interaction with its target substrates is regulated at the enzyme level.

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DO - 10.1074/jbc.M112.435842

M3 - Article

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Allosteric transitions direct protein tagging by PafA, the prokaryotic ubiquitin-like protein (Pup) ligase

Abstract

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