Febs Letters

doi: 10.1016/S0014-5793(10)00791-Xpmid: N/A

Devaux, Frédéric; Lelandais, Gaëlle; Garcia, Mathilde; Goussard, Sébastien; Jacq, Claude

doi: 10.1016/j.febslet.2010.09.030pmid: 20875412

This review focuses on the posttranscriptional processes which govern mitochondrial biogenesis, with a special emphasis on the asymmetric localization–translation of nuclear‐encoded mRNAs as an important regulatory step of the protein import process. We review how spatio‐temporal mRNA regulons help to elicit timely, versatile, and coordinated intracellular processes to assemble mitochondrial structures. Our current knowledge on the mitochondrial import of respiratory chain assembly factors and the role of the ribonucleic acid (RNA) binding protein Puf3 are presented. A connection with the target of rapamycine signalling pathway may explain how respiratory chain assembly senses environmental conditions via the protein import machinery.

Buechler, Christa; Wanninger, Josef; Neumeier, Markus

doi: 10.1016/j.febslet.2010.09.035pmid: 20875820

Adiponectin whose systemic levels are reduced in obesity‐related diseases ameliorates insulin sensitivity and regulates biological processes like apoptosis, proliferation, migration and inflammation. Adiponectin binds to adiponectin receptors, AdipoR1 and AdipoR2, which are ubiquitously expressed. Clathrin‐dependent endocytosis of AdipoR1 and adiponectin has been demonstrated to modulate adiponectin bioactivity. Recently, APPL1 has been identified as an AdipoR1 and AdipoR2 binding protein. Furthermore, activated protein kinase C1, endoplasmic reticulum protein 46 and protein kinase CK2β subunit form a complex with AdipoR1. This review summarizes recent studies exploiting heterologous expression of adiponectin receptors in yeast, and the type and function of the recently described adiponectin receptor associated proteins.

Knoop, Volker; Rüdinger, Mareike

doi: 10.1016/j.febslet.2010.09.041pmid: 20888816

A particular type of pentatricopeptide repeat (PPR) proteins with variable length of the 35 aa PPR motifs and conserved carboxyterminal extensions, named the PLS proteins, was so far exclusively identified in land plants. Several PLS proteins with such domain extensions (E, E+, DYW) were shown to be involved in plant organellar RNA editing but their evolutionary origin had remained enigmatic. We here report the first case of DYW‐type PLS proteins outside of the plant kingdom in the protist Naegleria gruberi and hypothesize on horizontal gene transfer in very early land plant evolution.

Naryzhny, Stanislav N.; Lee, Hoyun

doi: 10.1016/j.febslet.2010.09.021pmid: 20849852

MINT‐7995351: G3P (uniprotkb:P04406) and PCNA (uniprotkb:P12004) colocalize (MI:0403) by fluorescence microscopy (MI:0416)MINT‐7995334: ENOA (uniprotkb:P06733) and PCNA (uniprotkb:P12004) colocalize (MI:0403) by fluorescence microscopy (MI:0416)MINT‐7995368: ALDOA (uniprotkb:P04075) and PCNA (uniprotkb:P12004) colocalize (MI:0403) by fluorescence microscopy (MI:0416)MINT‐7995141: G3P (uniprotkb:P04406) binds (MI:0407) to PCNA (uniprotkb:P12004) by far western blotting (MI:0047)MINT‐7995182: ENOA (uniprotkb:P06733) binds (MI:0407) to PCNA (uniprotkb:P12004) by far western blotting (MI:0047)MINT‐7995132: G3P (uniprotkb:P04406) physically interacts (MI:0915) with PCNA (uniprotkb:P12004) by far western blotting (MI:0047)MINT‐7995228: PRDX6 (uniprotkb:P30041) physically interacts (MI:0915) with PCNA (uniprotkb:P12004) by far western blotting (MI:0047)MINT‐7995220: CAH2 (uniprotkb:P00918) physically interacts (MI:0915) with PCNA (uniprotkb:P12004) by far western blotting (MI:0047)MINT‐7995114: Triosephosphate isomerase (uniprotkb:P60174) binds (MI:0407) to PCNA (uniprotkb:P12004) by far western blotting (MI:0047)MINT‐7995244: K2C7 (uniprotkb:P08729) physically interacts (MI:0915) with PCNA (uniprotkb:P12004) by far western blotting (MI:0047)MINT‐7995252: ANXA2 (uniprotkb:P07355) physically interacts (MI:0915) with PCNA (uniprotkb:P12004) by far western blotting (MI:0047)MINT‐7995122: Triosephosphate isomerase (uniprotkb:P60174) physically interacts (MI:0915) with PCNA (uniprotkb:P12004) by far western blotting (MI:0047)MINT‐7995093: ALDOA (uniprotkb:P04075) physically interacts (MI:0915) with PCNA (uniprotkb:P12004) by far western blotting (MI:0047)MINT‐7995148: PGK1 (uniprotkb:P00558) physically interacts (MI:0915) with PCNA (uniprotkb:P12004) by far western blotting (MI:0047)MINT‐7995158: PGAM1 (uniprotkb:P18669) physically interacts (MI:0915) with PCNA (uniprotkb:P12004) by far western blotting (MI:0047)MINT‐7995166: PGAM1 (uniprotkb:P18669) binds (MI:0407) to PCNA (uniprotkb:P12004) by far western blotting (MI:0047)MINT‐7995105: ALDOA (uniprotkb:P04075) binds (MI:0407) to PCNA (uniprotkb:P12004) by far western blotting (MI:0047)MINT‐7995260: PPIA (uniprotkb:P62937) physically interacts (MI:0915) with PCNA (uniprotkb:P12004) by far western blotting (MI:0047)MINT‐7995173: ENOA (uniprotkb:P06733) physically interacts (MI:0915) with PCNA (uniprotkb:P12004) by far western blotting (MI:0047)MINT‐7995268: EF1A (uniprotkb:P68104) physically interacts (MI:0915) with PCNA (uniprotkb:P12004) by far western blotting (MI:0047)MINT‐7995236: MDHM (uniprotkb:P40926) physically interacts (MI:0915) with PCNA (uniprotkb:P12004) by far western blotting (MI:0047)MINT‐7995189: RSSA (uniprotkb:P08865) physically interacts (MI:0915) with PCNA (uniprotkb:P12004) by far western blotting (MI:0047)MINT‐7995282: PCNA (uniprotkb:P12004) physically interacts (MI:0915) with ALDOA (uniprotkb:P00883) and G3P (uniprotkb:P46406) by anti bait coimmunoprecipitation (MI:0006).

Ji, Jae-Hoon; Hwang, Hyo-In; Lee, Hee-Jae; Hyun, Sun-Yi; Kang, Hoe-Jin; Jang, Young-Joo

doi: 10.1016/j.febslet.2010.09.025pmid: 20869364

MINT‐7996345: PAK3 (uniprotkb:O75914) physically interacts (MI:0915) with PLK1 (uniprotkb:P53350) by pull down (MI:0096)

Engelbrecht, Stefanie; Kaltenborn, Eva; Griese, Matthias; Kern, Sunčana

doi: 10.1016/j.febslet.2010.09.026pmid: 20863830

MINT‐7996380, MINT‐7996593, MINT‐7996607: LAMP3 (uniprotkb:Q9UQV4) and ABCA3 (uniprotkb:Q99758) colocalize (MI:0403) by fluorescence microscopy (MI:0416)

Abe, Makoto; Suzuki, Hitoshi; Nishitsuji, Hironori; Shida, Hisatoshi; Takaku, Hiroshi

doi: 10.1016/j.febslet.2010.09.031pmid: 20869963

MINT‐7996852, MINT‐7996870, MINT‐7996886, MINT‐7996830: Rex (uniprotkb:P0C205) physically interacts (MI:0915) with Dicer (uniprotkb:Q9UPY3) by anti tag coimmunoprecipitation (MI:0007)

Yan, Jing; Di, Yujun; Shi, Huili; Rao, Hai; Huo, Keke

doi: 10.1016/j.febslet.2010.09.019pmid: 20849854

Previously, we defined SCY1‐like 1 binding protein 1 (SCYL1‐BP1) to be a substrate of Pirh2 that binds to mouse double minute gene number 2 (MDM2). In the current study, we found that an increase in SCYL1‐BP1 protein levels caused a parallel change in the amount of p53 protein due to the inhibition by SCYL‐BP1 of MDM2‐mediated p53 ubiquitination. SCYL1‐BP1 was not able to alter the ubiquitination of p53 by human papillomavirus protein E6, indicating that the effect was specific for MDM2. Increases in the level of SCYL1‐BP1 protein in cells led to the greater transcriptional activation of p21 and gadd45, reduced rate of cellular proliferation, increased levels of apoptosis and inhibition of tumorigenicity. Thus, we propose that SCYL1‐BP1 is a novel regulator of the MDM2‐p53 feedback loop and that it may be a potential tumor suppressor.

Liu, Yu; Wu, Na; Dong, Jie; Gao, Yaping; Zhang, Xin; Shao, Ningsheng; Yang, Guang

doi: 10.1016/j.febslet.2010.09.024pmid: 20854817

SsrA RNA (small stable RNA A), also known as tmRNA and 10Sa RNA, functions both as tRNA and mRNA through its unique structure. The carotenoid pigment is the eponymous feature of human pathogen Staphylococcus aureus. Here, we found that the pigment of the mutant strain with ssrA deletion was increased. Furthermore, it was demonstrated that ssrA could act as an antisense RNA aside from its well‐known biological function, and crtMN, encoding two essential enzymes for the pigment synthesis, was identified as target of ssrA. Further investigation showed ssrA could specifically base pair with the RBS (ribosomal binding site) region of the crtMN mRNA. Our results revealed a new mechanism by which ssrA regulated the biosynthesis of pigment in S. aureus.