Mitochondrial and chloroplast localization of FtsH-like proteins in sugarcane based on their phylogenetic profile

Marbach, Phellippe Arthur Santos; Coelho, Alexandre Siqueira Guedes; Silva-Filho, Marcio C.

doi:10.1590/s1415-47572001000100025

Cited by 7 publications

(12 citation statements)

References 30 publications

(43 reference statements)

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“…Despite the similar membrane topology, complementation studies suggest that The subcellular localization of AtFtsH4 and AtFtsH11 was uncertain according to organelletargeting programs (Sokolenko et al, 2002;Yu et al, 2004). Phylogenetic studies indicate that both proteins have mitochondrial origin (Marbach et al, 2001). Contradictory experimental data have been published regarding the subcellular localization of these proteases.…”

Section: Discussionmentioning

confidence: 99%

Plant Mitochondria Contain at Least Two i-AAA-like Complexes

Urantówka

Knorpp²,

Olczak

et al. 2005

Plant Mol Biol

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The FtsH proteases, also called AAA proteases, are membrane-bound ATP-dependent metalloproteases. The Arabidopsis genome contains a total of 12 FtsH-like genes. Two of them, AtFtsH4 and AtFtsH11, encode proteins with a high similarity to Yme1p, a subunit of the i-AAA complex in yeast mitochondria. Phylogenetic analysis groups the AtFtsH4, AtFtsH11 and Yme1 proteins together, with AtFtsH4 being the most similar to Yme1. Using immunological method we demonstrate here that AtFtsH4 is an exclusively mitochondrial protein while AtFtsH11 is found in both chloroplasts and mitochondria. AtFtsH4 and AtFtsH11 proteases are integral parts of the inner mitochondrial membrane and expose their catalytic sites towards the intermembrane space, same as yeast i-AAA. Database searches revealed that orthologs of AtFtsH4 and AtFtsH11 are present in both monocotyledonous and dicotyledonous plants. The two plant i-AAA proteases differ significantly in their termini: the FtsH4 proteins have a characteristic alanine stretch at the C-terminal end while FtsH11s have long N-terminal extensions. Blue-native gel electrophoresis revealed that AtFtsH4 and AtFtsH11 form at least two complexes with apparent molecular masses of about 1500 kDa. This finding implies that plants, in contrast to fungi and metazoa, have more than one complex with a topology similar to that of yeast i-AAA.

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Section: Discussionmentioning

confidence: 99%

Plant Mitochondria Contain at Least Two i-AAA-like Complexes

Urantówka

Knorpp²,

Olczak

et al. 2005

Plant Mol Biol

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“…The i-AAA proteases span the inner mitochondrial membrane and are exposed to the intermembrane space, while the m-AAA proteases have their active site exposed to the organellar matrix. Three plastid FtsH groups (P1, P2 and P3) have been described on the basis of sequence identity and hydropathy index [39,40]. …”

Section: Introductionmentioning

confidence: 99%

An FtsH Protease Is Recruited to the Mitochondrion of Plasmodium falciparum

et al. 2013

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The two organelles, apicoplast and mitochondrion, of the malaria parasite Plasmodium falciparum have unique morphology in liver and blood stages; they undergo complex branching and looping prior to division and segregation into daughter merozoites. Little is known about the molecular processes and proteins involved in organelle biogenesis in the parasite. We report the identification of an AAA+/FtsH protease homolog (PfFtsH1) that exhibits ATP- and Zn2+-dependent protease activity. PfFtsH1 undergoes processing, forms oligomeric assemblies, and is associated with the membrane fraction of the parasite cell. Generation of a transfectant parasite line with hemagglutinin-tagged PfFtsH1, and immunofluorescence assay with anti-PfFtsH1 Ab demonstrated that the protein localises to P. falciparum mitochondria. Phylogenetic analysis and the single transmembrane region identifiable in PfFtsH1 suggest that it is an i-AAA like inner mitochondrial membrane protein. Expression of PfFtsH1 in Escherichia coli converted a fraction of bacterial cells into division-defective filamentous forms implying a sequestering effect of the Plasmodium factor on the bacterial homolog, indicative of functional conservation with EcFtsH. These results identify a membrane-associated mitochondrial AAA+/FtsH protease as a candidate regulatory protein for organelle biogenesis in P. falciparum.

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“…Among A. thaliana FtsH‐like proteases, three members, AtFtsH3, AtFtsH10 and AtFtsH4 are targeted into mitochondria based on an in vivo transient expression assay using green fluorescent protein fusion system in suspension‐cultured tobacco cells (Sakamoto et al 2003). Phylogenetic studies indicate that AtFtsH3 and AtFtsH10 are closely related (Marbach et al 2001, Sakamoto et al 2003, Yu et al 2004). On the other hand, mitochondrial localized AtFtsH4 groups together with chloroplastic AtFtsH11 suggesting that these proteases are somewhat related, but to a lesser extent than the AtFtsH3 and FtsH10 pair.…”

Section: Introductionmentioning

confidence: 99%

ATP‐dependent proteases in plant mitochondria: What do we know about them today?

Jańska

2004

Physiologia Plantarum

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Lon‐, Clp‐ and FtsH‐like proteases, members of three families of ATP‐dependent proteases derived from bacterial ancestors, have been identified in plant mitochondria. Classifications of mitochondrial‐specific paralogues of plant ATP‐dependent proteases, based on targeting prediction programs and different experimental methods, are compared. Accumulating evidence points to similarities in the structure and the mechanisms of action used by various ATP‐dependent proteases. Therefore, before focusing on plant mitochondrial ATP‐dependent proteases, the paper discusses general features of ATP‐dependent proteases. To date, information about structure and function of plant mitochondrial Lon‐like, Clp‐like and FtsH‐like proteases is rather scarce, but indicates that these enzymes, like their bacterial and eukaryotic homologues, combine proteolytic and chaperone‐like activities to form mitochondrial protein quantity and quality control system in plants.

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Mitochondrial and chloroplast localization of FtsH-like proteins in sugarcane based on their phylogenetic profile

Cited by 7 publications

References 30 publications

Plant Mitochondria Contain at Least Two i-AAA-like Complexes

Plant Mitochondria Contain at Least Two i-AAA-like Complexes

An FtsH Protease Is Recruited to the Mitochondrion of Plasmodium falciparum

ATP‐dependent proteases in plant mitochondria: What do we know about them today?

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