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1.
Osafune Tetsuaki; Mihara Sayoko; Hase Eiji; Ohkuro Isamu 《Plant & cell physiology》1972,13(2):211-227
Changes in subcellular structures during the entire vegetativecell cycle of Chlamydomonas reinhardi Dangeard in synchronousculture were followed with an electron microscope. Giant mitochondriaof various shapes were temporarily formed, probably by fusionof smaller mitochondria, in the algal cells at an intermediatestage of the growth phase of the cell cycle. Formation of giantmitochondria was accompanied by a marked decrease in the oxygen-uptakeactivity of cells. Giant mitochondria divided into smaller formsconcurrently with a re-increase in the oxygen-uptake activityof cells. Some characteristics of changes in the structuresof chloroplast, the nucleus, the endoplasmic reticula, flagellaand dictyosomes are described.
1 This work was reported in part at the 35th Annual Meetingof the Botanical Society of Japan, October 1970. (Received October 13, 1971; ) 相似文献
2.
Cytosolic and mitochondrial surface factor-independent import of a synthetic peptide into mitochondria. 总被引:1,自引:0,他引:1 下载免费PDF全文
We chemically synthesized a peptide, 11 beta-45, which was composed of 45 amino acid residues including the whole extension peptide and some of the mature portion of bovine cytochrome P-450(11 beta) precursor. 11 beta-45 was imported into mitochondria in vitro depending on the mitochondrial membrane potential, but its import did not require extramitochondrial ATP. Although cytosolic protein factors in the high speed supernatant of reticulocyte lysate are known to stimulate the import of various precursor proteins into mitochondria, the import of 11 beta-45 was not stimulated by cytosolic factors in reticulocyte lysate. The import of the peptide did not require mitochondrial surface protein components because its import was not affected by trypsin treatment of mitochondria. On the other hand, trypsin treatment of mitoplasts resulted in a great reduction in the import of the peptide, indicating that 11 beta-45 interacts during the import process with some protein components located inside mitochondria. These observations indicated that the peptide 11 beta-45 was imported via the potential-dependent pathway as in the case of precursor proteins, but skipped the interactions with cytosolic factors and mitochondrial surface components normally required for the import of precursor proteins. 相似文献
3.
4.
Cytoplasmic chaperones determine the targeting pathway of precursor proteins to mitochondria. 总被引:6,自引:1,他引:5 下载免费PDF全文
Two ATP-dependent cytosolic chaperones, mitochondrial import stimulation factor (MSF) and hsp70, are known to be involved in the import of precursor proteins into mitochondria. Hsp70 generally recognizes unfolded proteins, while MSF specifically recognizes mitochondrial precursor proteins and targets them to mitochondria in a NEM-sensitive manner. Here we analyzed the relative contribution of these chaperones in the import process and confirmed that the precursor proteins are targeted to mitochondria via two distinct pathways: one requiring MSF and the other requiring hsp70. Both pathways depend on distinct proteinaceous components of the outer mitochondrial membrane. The MSF-dependent pathway is NEM-sensitive and requires the hydrolysis of extra-mitochondrial ATP for the release of MSF from the mitochondrial import receptor, whereas the hsp70-dependent pathway is NEM-sensitive and does not require extra-mitochondrial ATP. The NEM-insensitive, hsp70-dependent import became NEM-sensitive depending on the amount of MSF added. The relative importance of the two pathways appears to be determined by the affinities of MSF and hsp70 for the precursor proteins. 相似文献
5.
Hisakazu Mihara Kin-Ya Tomizaki Norikazu Nishino Tsutomu Fujimoto Haruhiko Tamaoki Yuji Kobayashi 《Biopolymers》1994,34(7):963-967
A model 16-peptide of endothelin-1 (MET-1), which has the minimized sequence homology to the corresponding pan of endothelin-1 (ET-1), was designed to confirm the cystine-stabilized α-helix motif. The model structure consists of an extended structure, a β-turn part, and an α-helix structure that is stabilized by two disulfide bonds. The α-helix segment was designed to emphasize the amphiphilic nature. In order to combine the extended structure and the α-helix segment, a D -Ala-Pro sequence was selected to fix the β-turn. The model endothelin 16-peptide amide was synthesized by solid-phase synthesis on a 4-methylbenzhydrylamine resin. Its conformation was examined by CD and two-dimensional (2D) 1H-nmr measurements. MET-1 showed similar CD patterns to ET-1 in both buffer and 50% aqueous trifluoroethanol solution. The 2D nmr experiments in 50% aqueous ethylene glycol revealed that MET-1 closely resembles the conformation of ET-1 with an extended structure, an α-helix, and a β-turn unit in the same position of the sequence. Furthermore, model peptides without disulfide bond(s) could not assume a stable structure in aqueous solution, while they did have similar α-helical content in 50% trifluoroethanol with MET-1. When the two disulfide bridges were simultaneously formed, the peptide with the correct disulfide bonds (MET-1) was obtained in threefold excess to the isomer (apamin type. MET-2). These findings obtained by the modeling of ET-1 showed an important role for the stabilization of peptide conformation with disulfide bonds. © 1994 John Wiley & Sons, Inc. 相似文献
6.
7.
We characterized the endothelin (ET) receptor in Girardi heart (GH) cells derived from human atrium. The ET isopeptides ET-1, ET-2 and ET-3 induced the monotonous and long-lasting rise in cytosolic free Ca2+ concentration [( Ca2+]i) with almost the same potency in GH cells. Scatchard analysis of [125I]ET-1 and [125I]ET-3 binding revealed that GH cells have almost the same number of binding sites for either labeled ligand. All ET isopeptides displaced either [125I]ET-1 or [125I]ET-3 binding in GH cells almost equipotently. These results reveal that the functional ET receptors in GH cells are of the ETB-type. GH cells are the first cell line to be found to express the functional ETB-receptor. 相似文献
8.
K Mihara 《Journal of biochemistry》1990,108(6):1022-1029
9.
Structural requirements for interruption of protein translocation across rough endoplasmic reticulum membrane 总被引:5,自引:0,他引:5
Co-translational translocation of proteins across the membrane of rough endoplasmic reticulum (ER) is interrupted by particular amino acid sequences, which are functionally termed "stop-transfer sequence." We analyzed the structural requirements for the interruption of the peptide translocation. By the manipulation of the cDNA of interleukin 2 (IL2), which passes through ER membrane co-translationally, the middle portion of the IL2 molecule was replaced with systematically altered hydrophobic segments, leucine, alanine, or leucine/alanine mixed clusters. Furthermore, charged amino acid residues were introduced just downstream of the hydrophobic segments. These modified IL2 peptides were synthesized with wheat germ cell-free system in the presence of rough microsomes and the topology of the peptides in the microsomes was assessed by post-translational digestion with proteinase K. We obtained the following results. (i) Each modified protein was processed to the mature form but the extent of stop-translocation varied widely. The ratio of the stopped to the translocated products increased as the length and hydrophobicity of the inserted segment increased. (ii) Shorter hydrophobic segments than naturally occurring native transmembrane segment promoted stop-translocation. (iii) Proteins with hydrophobic segments followed by positive charges were more efficiently stop-translocated than those having negative charges. (iv) If the hydrophobicity of the segment was sufficiently high, the positive charges after the segment were not essential for stop-translocation. We also suggest that the stop-transfer process includes protein-protein interaction between the hydrophobic segment and translocation channel. 相似文献
10.
Hiroshi Nakayasu Katsuyoshi Mihara Ryo Sato 《Biochemical and biophysical research communications》1978,83(2):697-703
A membrane-bound aldehyde dehydrogenase was solubilized from rat liver microsomes and purified about 150-fold by chromatography on ω-aminohexyl- and 5′-AMP-Sepharose columns with a recovery of about 40%. The purified enzyme was homogeneous upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis and its monomeric molecular weight was estimated to be 51,000. In aqueous solution, it existed as large, polymeric aggregates. Its activity towards straight-chain aliphatic aldehydes increased as their carbon chain length was increased at least up to dodecanal, whereas aldehyde dehydrogenase in the cytosolic fraction of rat liver was most active with hexanal as substrate. 相似文献