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Processing and Degradation of Chloroplast Extension Peptides

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Book cover Plastid Biology

Part of the book series: Advances in Plant Biology ((AIPB,volume 5))

Abstract

Most chloroplast proteins are synthesized as larger precursors with cleavable extension peptides. These extensions include import signals called transit peptides, export signals for thylakoid transfer, and the C-terminal extension of the chloroplast-encoded D1 subunit of the photosystem II. Transit peptides are necessary for transport of nuclear-encoded proteins from the cytoplasm across the double-membrane envelope, and are cleaved off by Stromal Processing Peptidase (SPP) in the stroma. Further degradation of transit peptides involves SPP and Presequence Protease (PreP). Thylakoid-transfer sequences are required for correct intraorganellar protein sorting and cleaved by Thylakoidal Processing Peptidase (TPP) in the thylakoid lumen. The C-terminal extension of the D1 protein is not required for precursor targeting and integration into the protein complex; however its removal by Carboxyl-terminal peptidase called CtpA in the thylakoid lumen is needed for proper formation of the photosystem II Mn4CaO5 cluster. Biochemical studies in the 1980s–1990s defined basic properties of SPP, TPP and CtpA, while PreP was discovered in the early 2000s. Recent molecular genetic studies demonstrated physiological importance as well as some unprecedented functions of these enzymes. This chapter gives a comprehensive survey on processing and degradation of chloroplast extension peptides. The emphasis is on biochemical, molecular and evolutionary aspects of proteases. The significances of the presence and processing of these extension peptides are also discussed.

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Abbreviations

Aβ:

Amyloid beta peptide

ACP:

Acyl Carrier Protein

AD:

Alzheimer’s disease

cpSEC:

Chloroplastic SEC

cpSRP:

Chloroplastic Signal Recognition Particle

cpTAT:

Chloroplastic Twine-Arginine-Transport

CtpA:

The D1 Carboxyl-terminal peptidase

GFP:

Green Fluorescent Protein

HSP21:

Heat Shock Protein 21

MPP:

Mitochondrial Processing Peptidase

MS:

Mass Spectrometry

OEC:

Oxygen Evolving Complex

Plsp:

Plastidic type I signal peptidase

PreP:

Presequence Protease

RBCS:

Small subunit of Rubisco

ROS:

Reactive Oxygen Species

Rubisco:

Ribulose-1,5-bisphosphate carboxylase/oxygenase

S2P:

Site-2-Protease

SPase I:

Type I signal peptidase

SPP:

Stromal Processing Peptidase

SStpPs:

Transit peptide of the RBCS precursor

TIC:

Transocon at the Inner-envelope-membrane of Chloroplasts

TOC:

Translocon at the Outer-envelope-membrane of Chloroplasts

TPP:

Thylakoidal Processing Peptidase

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Acknowledgements

The work on TPP in the Inoue laboratory has been supported by the Division of Chemical Sciences, Geosciences, and Biosciences, Office of Basic Energy Sciences of the U.S. Department of Energy through Grant DE-FG02-08ER15963. The work on PreP in the Glaser laboratory was supported by research grants from the Swedish Research Council (VR-NT 2009-5641), Carl Tryggers Foundation and Alzheimerfonden.

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Authors and Affiliations

  1. Department of Plant Sciences, University of California, One Shields Avenue, Davis, CA 95616, USA

    Kentaro Inoue

  2. Department of Biochemistry and Biophysics, Stockholm University, SE-106 91, Stockholm, Sweden

    Elzbieta Glaser

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  1. Kentaro Inoue
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Correspondence to Kentaro Inoue .

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Editors and Affiliations

  1. Department of Plant Biology, Univeristy of California-Davis, Davis, California, USA

    Steven M. Theg

  2. Physiologie Membranaire et Moléculaire du Chloroplaste, Institut de Biologie Physico-Chimique, Paris, France

    Francis-André Wollman

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Inoue, K., Glaser, E. (2014). Processing and Degradation of Chloroplast Extension Peptides. In: Theg, S., Wollman, FA. (eds) Plastid Biology. Advances in Plant Biology, vol 5. Springer, New York, NY. https://doi.org/10.1007/978-1-4939-1136-3_12

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