LACTB is a filament-forming protein localized  in mitochondria

Zydrune Polianskyte-Prause; Nina Peitsaro; Arvydas Dapkunas; Julius Liobikas; Rabah Soliymani; Maciej Lalowski; Oliver Speer; Jani Seitsonen; Sarah Jane Butcher; Grazia M Cereghetti; Matts D Linder; Michael Merckel; James Thompson; Ove Eriksson-Rosenberg

doi:10.1073/pnas.0906734106

LACTB is a filament-forming protein localized in mitochondria

Zydrune Polianskyte-Prause, Nina Peitsaro, Arvydas Dapkunas, Julius Liobikas, Rabah Soliymani, Maciej Lalowski, Oliver Speer, Jani Seitsonen, Sarah Jane Butcher, Grazia M Cereghetti, Matts D Linder, Michael Merckel, James Thompson, Ove Eriksson-Rosenberg

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

Abstract

LACTB is a mammalian active-site serine protein that has evolved from a bacterial penicillin-binding protein. Penicillin-binding proteins are involved in the metabolism of peptidoglycan, the major bacterial cell wall constituent, implying that LACTB has been endowed with novel biochemical properties during eukaryote evolution. Here we demonstrate that LACTB is localized in the mitochondrial intermembrane space, where it is polymerized into stable filaments with a length extending more than a hundred nanometers. We infer that LACTB, through polymerization, promotes intramitochondrial membrane organization and micro-compartmentalization. These findings have implications for our understanding of mitochondrial evolution and function.

Original language	English
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	106
Issue number	45
Pages (from-to)	18960-18965
Number of pages	6
ISSN	0027-8424
DOIs	https://doi.org/10.1073/pnas.0906734106
Publication status	Published - 2009
MoE publication type	A1 Journal article-refereed

Fields of Science

118 Biological sciences

Access to Document

10.1073/pnas.0906734106

Cite this

Polianskyte-Prause, Z., Peitsaro, N., Dapkunas, A., Liobikas, J., Soliymani, R., Lalowski, M., Speer, O., Seitsonen, J., Butcher, S. J., Cereghetti, G. M., Linder, M. D., Merckel, M., Thompson, J., & Eriksson-Rosenberg, O. (2009). LACTB is a filament-forming protein localized in mitochondria. Proceedings of the National Academy of Sciences of the United States of America, 106(45), 18960-18965. https://doi.org/10.1073/pnas.0906734106

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title = "LACTB is a filament-forming protein localized in mitochondria",

abstract = "LACTB is a mammalian active-site serine protein that has evolved from a bacterial penicillin-binding protein. Penicillin-binding proteins are involved in the metabolism of peptidoglycan, the major bacterial cell wall constituent, implying that LACTB has been endowed with novel biochemical properties during eukaryote evolution. Here we demonstrate that LACTB is localized in the mitochondrial intermembrane space, where it is polymerized into stable filaments with a length extending more than a hundred nanometers. We infer that LACTB, through polymerization, promotes intramitochondrial membrane organization and micro-compartmentalization. These findings have implications for our understanding of mitochondrial evolution and function.",

keywords = "118 Biological sciences",

author = "Zydrune Polianskyte-Prause and Nina Peitsaro and Arvydas Dapkunas and Julius Liobikas and Rabah Soliymani and Maciej Lalowski and Oliver Speer and Jani Seitsonen and Butcher, {Sarah Jane} and Cereghetti, {Grazia M} and Linder, {Matts D} and Michael Merckel and James Thompson and Ove Eriksson-Rosenberg",

year = "2009",

doi = "10.1073/pnas.0906734106",

language = "English",

volume = "106",

pages = "18960--18965",

journal = "Proceedings of the National Academy of Sciences of the United States of America",

issn = "0027-8424",

publisher = "National Academy of Sciences",

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Polianskyte-Prause, Z , Peitsaro, N, Dapkunas, A, Liobikas, J, Soliymani, R, Lalowski, M, Speer, O, Seitsonen, J, Butcher, SJ, Cereghetti, GM, Linder, MD, Merckel, M, Thompson, J & Eriksson-Rosenberg, O 2009, 'LACTB is a filament-forming protein localized in mitochondria', Proceedings of the National Academy of Sciences of the United States of America, vol. 106, no. 45, pp. 18960-18965. https://doi.org/10.1073/pnas.0906734106

TY - JOUR

T1 - LACTB is a filament-forming protein localized in mitochondria

AU - Polianskyte-Prause, Zydrune

AU - Peitsaro, Nina

AU - Dapkunas, Arvydas

AU - Liobikas, Julius

AU - Soliymani, Rabah

AU - Lalowski, Maciej

AU - Speer, Oliver

AU - Seitsonen, Jani

AU - Butcher, Sarah Jane

AU - Cereghetti, Grazia M

AU - Linder, Matts D

AU - Merckel, Michael

AU - Thompson, James

AU - Eriksson-Rosenberg, Ove

PY - 2009

Y1 - 2009

N2 - LACTB is a mammalian active-site serine protein that has evolved from a bacterial penicillin-binding protein. Penicillin-binding proteins are involved in the metabolism of peptidoglycan, the major bacterial cell wall constituent, implying that LACTB has been endowed with novel biochemical properties during eukaryote evolution. Here we demonstrate that LACTB is localized in the mitochondrial intermembrane space, where it is polymerized into stable filaments with a length extending more than a hundred nanometers. We infer that LACTB, through polymerization, promotes intramitochondrial membrane organization and micro-compartmentalization. These findings have implications for our understanding of mitochondrial evolution and function.

AB - LACTB is a mammalian active-site serine protein that has evolved from a bacterial penicillin-binding protein. Penicillin-binding proteins are involved in the metabolism of peptidoglycan, the major bacterial cell wall constituent, implying that LACTB has been endowed with novel biochemical properties during eukaryote evolution. Here we demonstrate that LACTB is localized in the mitochondrial intermembrane space, where it is polymerized into stable filaments with a length extending more than a hundred nanometers. We infer that LACTB, through polymerization, promotes intramitochondrial membrane organization and micro-compartmentalization. These findings have implications for our understanding of mitochondrial evolution and function.

KW - 118 Biological sciences

U2 - 10.1073/pnas.0906734106

DO - 10.1073/pnas.0906734106

M3 - Article

SN - 0027-8424

VL - 106

SP - 18960

EP - 18965

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

IS - 45

ER -