Extremely large and slowly processed precursors to the Euglena light-harvesting chlorophyll a/b binding proteins of photosystem II.
Extremely large and slowly processed precursors to the Euglena light-harvesting chlorophyll a/b binding proteins of photosystem II.
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光系统 II 的眼虫捕光叶绿素 a/b 结合蛋白的极大且缓慢加工的前体。
DOI:
10.1073/pnas.85.14.5117
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发表时间:
1988
影响因子:
11.1
通讯作者:
Schwartzbach,SD
中科院分区:
文献类型:
--
作者:
Rikin,A;Schwartzbach,SD
Antibody to theEuglenalight-harvesting chlorophyll a/b binding protein of photosystem II (LHCPII) immunoprecipitated 207-, 161-, 122-, and 110-kDa proteins from totalEuglenaproteins pulse-labeled for 10 min with [35S]sulfate. The 25.6- and 27.2-kDa LHCPII were barely detectable in the immunoprecipitate. During a 40-min chase with unlabeled sulfate, the amount of radioactivity in the high molecular mass proteins decreased, and the amount of radioactivity in the 25.6- and 27.2-kDa LHCPII increased with kinetics consistent with a precursor-product relationship. The half-life of the high molecular mass proteins was ≈20 min. The major proteins immunoprecipitated from a nuclease-treated rabbit reticulocyte cell-free translation system programmed withEuglenawhole cell or poly(A)+RNA had molecular masses corresponding to the molecular masses of the proteins immunoprecipitated from the pulse-labeledin vivotranslation products. RNAs of 6.6 and 8.3 kilobases were the onlyEuglenawhole cell and poly(A)+RNAs that hybridized to a 0.7-kilobaseEcoRI-BamHI fragment of plasmid pAB165, which contains a portion of the coding sequence forArabidopsisLHCPII. RNAs of this size are more than sufficient to code for proteins of 207 kDa. Taken together, these findings demonstrate that the LHCPIIs ofEuglenaare initially synthesized as slowly processed precursors with molecular masses of 207, 161, 122, and 110 kDa.
DOI:
--
发表时间:
1984
期刊:
Advances in Agricultural Biotechnology
影响因子:
--
作者:
Kazuo Shibata
通讯作者:
Kazuo Shibata
影响因子:
4.3
作者:
H. Sambrook
通讯作者:
H. Sambrook