The Known, the New, and a Possible Surprise: A Re-Evaluation of the Nucleomorph-Encoded Proteome of Cryptophytes

被引:6
作者
Zauner, Stefan [1 ]
Heimerl, Thomas [2 ]
Moog, Daniel [1 ,2 ]
Maier, Uwe G. [1 ,2 ]
机构
[1] Philipps Univ Marburg, Dept Cell Biol, Marburg, Germany
[2] Philipps Univ Marburg, SYNMIKRO Res Ctr, Marburg, Germany
关键词
cryptomonad; nucleomorph; nucleomorph-encoded proteins; periplastid compartment; plastid; ENDOPLASMIC-RETICULUM; GENOME SEQUENCE; PROTEINS; COMPARTMENT; PLASTIDS; REVEALS; IMPORT; ULTRASTRUCTURE; CHLOROPLASTS; REQUIRES;
D O I
10.1093/gbe/evz109
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
Nucleomorphs are small nuclei that evolved from the nucleus of former eukaryotic endosymbionts of cryptophytes and chlorarachniophytes. These enigmatic organelles reside in their complex plastids and harbor the smallest and most compacted eukaryotic genomes investigated so far. Although the coding capacity of the nucleomorph genomes is small, a significant percentage of the encoded proteins (predicted nucleomorph-encoded proteins, pNMPs) is still not functionally annotated. We have analyzed pNMPs with unknown functions via Phyre(2), a bioinformatic tool for prediction and modeling of protein structure, resulting in a functional annotation of 215 pNMPs out of 826 uncharacterized open reading frames of cryptophytes. The newly annotated proteins are predicted to participate in nucleomorph-specific functions such as chromosome organization and expression, as well as in modification and degradation of nucleomorph-encoded proteins. Additionally, we have functionally assigned nucleomorph-encoded, putatively plastid-targeted proteins among the reinvestigated pNMPs. Hints for a putative function in the periplastid compartment, the cytoplasm surrounding the nucleomorphs, emerge from the identification of pNMPs that might be homologs of endomembrane system-related proteins. These proteins are discussed in respect to their putative functions.
引用
收藏
页码:1618 / 1629
页数:12
相关论文
共 51 条
[1]   The dynamin-like GTPase Sey1p mediates homotypic ER fusion in S. cerevisiae [J].
Anwar, Kamran ;
Klemm, Robin W. ;
Condon, Amanda ;
Severin, Katharina N. ;
Zhang, Miao ;
Ghirlando, Rodolfo ;
Hu, Junjie ;
Rapoport, Tom A. ;
Prinz, William A. .
JOURNAL OF CELL BIOLOGY, 2012, 197 (02) :209-217
[2]   Chaperoning SNARE assembly and disassembly [J].
Baker, Richard W. ;
Hughson, Frederick M. .
NATURE REVIEWS MOLECULAR CELL BIOLOGY, 2016, 17 (08) :465-479
[3]   Bipartite signals mediate subcellular targeting of tail-anchored membrane proteins in Saccharomyces cerevisiae [J].
Beilharz, T ;
Egan, B ;
Silver, PA ;
Hofmann, K ;
Lithgow, T .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (10) :8219-8223
[4]   Complementation of a phycocyanin-bilin lyase from Synechocystis sp PCC 6803 with a nucleomorph-encoded open reading frame from the cryptophyte Guillardia theta [J].
Bolte, Kathrin ;
Kawach, Oliver ;
Prechtl, Julia ;
Gruenheit, Nicole ;
Nyalwidhe, Julius ;
Maier, Uwe-G .
BMC PLANT BIOLOGY, 2008, 8 (1)
[5]   Nuclear pore complex integrity requires Lnp1, a regulator of cortical endoplasmic reticulum [J].
Casey, Amanda K. ;
Chen, Shuliang ;
Novick, Peter ;
Ferro-Novick, Susan ;
Wente, Susan R. .
MOLECULAR BIOLOGY OF THE CELL, 2015, 26 (15) :2833-2844
[6]   Membrane heredity and early chloroplast evolution [J].
Cavalier-Smith, T .
TRENDS IN PLANT SCIENCE, 2000, 5 (04) :174-182
[7]   Kingdom Chromista and its eight phyla: a new synthesis emphasising periplastid protein targeting, cytoskeletal and periplastid evolution, and ancient divergences [J].
Cavalier-Smith, Thomas .
PROTOPLASMA, 2018, 255 (01) :297-357
[8]   Endoplasmic Reticulum Targeting and Insertion of Tail-Anchored Membrane Proteins by the GET Pathway [J].
Denic, Vladimir ;
Doetsch, Volker ;
Sinning, Irmgard .
COLD SPRING HARBOR PERSPECTIVES IN BIOLOGY, 2013, 5 (08)
[9]   The highly reduced genome of an enslaved algal nucleus [J].
Douglas, S ;
Zauner, S ;
Fraunholz, M ;
Beaton, M ;
Penny, S ;
Deng, LT ;
Wu, XN ;
Reith, M ;
Cavalier-Smith, T ;
Maier, UG .
NATURE, 2001, 410 (6832) :1091-1096
[10]   Apaf1 plays a pro-survival role by regulating centrosome morphology and function [J].
Ferraro, Elisabetta ;
Pesaresi, Maria Grazia ;
De Zio, Daniela ;
Cencioni, Maria Teresa ;
Gortat, Anne ;
Cozzolino, Mauro ;
Berghella, Libera ;
Salvatore, Anna Maria ;
Oettinghaus, Bjorn ;
Scorrano, Luca ;
Perez-Paya, Enrique ;
Cecconi, Francesco .
JOURNAL OF CELL SCIENCE, 2011, 124 (20) :3450-3463