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1.
Mol Plant ; 15(9): 1470-1487, 2022 09 05.
Artigo em Inglês | MEDLINE | ID: mdl-35957532

RESUMO

During adaptive radiation, mitochondria have co-evolved with their hosts, leading to gain or loss of subunits and assembly factors of respiratory complexes. Plant mitochondrial complex I harbors ∼40 nuclear- and 9 mitochondrial-encoded subunits, and is formed by stepwise assembly during which different intermediates are integrated via various assembly factors. In mammals, the mitochondrial complex I intermediate assembly (MCIA) complex is required for building the membrane arm module. However, plants have lost almost all of the MCIA complex components, giving rise to the hypothesis that plants follow an ancestral pathway to assemble the membrane arm subunits. Here, we characterize a maize crumpled seed mutant, crk1, and reveal by map-based cloning that CRK1 encodes an ortholog of human complex I assembly factor 1, zNDUFAF1, the only evolutionarily conserved MCIA subunit in plants. zNDUFAF1 is localized in the mitochondria and accumulates in two intermediate complexes that contain complex I membrane arm subunits. Disruption of zNDUFAF1 results in severe defects in complex I assembly and activity, a cellular bioenergetic shift to aerobic glycolysis, and mitochondrial vacuolation. Moreover, we found that zNDUFAF1, the putative mitochondrial import inner membrane translocase ZmTIM17-1, and the isovaleryl-coenzyme A dehydrogenase ZmIVD1 interact each other, and could be co-precipitated from the mitochondria and co-migrate in the same assembly intermediates. Knockout of either ZmTIM17-1 or ZmIVD1 could lead to the significantly reduced complex I stability and activity as well as defective seeds. These results suggest that zNDUFAF1, ZmTIM17-1 and ZmIVD1 probably form an MCIA-like complex that is essential for the biogenesis of mitochondrial complex I and seed development in maize. Our findings also imply that plants and mammals recruit MCIA subunits independently for mitochondrial complex I assembly, highlighting the importance of parallel evolution in mitochondria adaptation to their hosts.


Assuntos
Complexo I de Transporte de Elétrons , Zea mays , Núcleo Celular/metabolismo , Complexo I de Transporte de Elétrons/genética , Complexo I de Transporte de Elétrons/metabolismo , Humanos , Mitocôndrias/metabolismo , Proteínas Mitocondriais/genética , Proteínas Mitocondriais/metabolismo , Sementes/metabolismo , Zea mays/metabolismo
2.
Int J Biol Macromol ; 106: 955-962, 2018 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-28830776

RESUMO

The effects of six nucleating agents (NAs), i.e., orotic acid (OA), potassium salt of 3,5-bis(methoxycarbonyl)benzenesulfonate (LAK-301), substituted-aryl phosphate salts (TMP-5), talc (TALC), N'1,N'6-dibenzoyladipohydrazide (TMC-306) and N1,N1'-(ethane-1,2-diyl)bis(N2-phenyloxalamide) (OXA), on the crystallization behavior of poly(lactic acid) (PLA) were compared by DSC. Under the same dosing of 0.5wt%, the nucleation effect of the NAs for PLA declines in the order of TMC-306≈OXA>TALC≫TMP-5≈LAK-301≈OA. The nucleation efficiency (NE) of TMC-306 and OXA is around 50%, which is almost 2 times of the NE of TALC. In the best case of the PLA/TMC-0.5% sample, the half-time of crystallization decreases from 30s to 9s with decreasing the crystallization temperature from 120°C to 100°C, which is of great significance to the fast production of highly crystallized PLA materials. As high-efficient NAs, TMC-306 and OXA are able to accelerate the crystallization rate of PLA even upon fast cooling at 50°C/min, while make no difference on PLA crystal form, as identified by WAXD. DMA analysis shows that the storage modulus of PLA is significantly improved by TMC-306 and OXA.


Assuntos
Cristalização , Poliésteres/química , Polímeros/química , Benzamidas/química , Benzamidas/farmacologia , Varredura Diferencial de Calorimetria , Catálise , Ácido Orótico/química , Ácido Orótico/farmacologia , Poliésteres/síntese química , Polímeros/síntese química , Talco/química , Talco/farmacologia , Temperatura , Difração de Raios X
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