C2 domain protein MIN1 promotes eyespot organization in Chlamydomonas reinhardtii.
C2 domain protein MIN1 promotes eyespot organization in Chlamydomonas reinhardtii.
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C2 结构域蛋白 MIN1 促进莱茵衣藻的眼斑组织。
DOI:
10.1128/ec.00118-08
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发表时间:
2008
期刊:
影响因子:
--
通讯作者:
Dieckmann,CarolL
中科院分区:
文献类型:
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作者:
Mittelmeier,TelsaM;Berthold,Peter;Danon,Avihai;Lamb,MaryRose;Levitan,Alexander;Rice,MichaelE;Dieckmann,CarolL
Assembly and asymmetric localization of the photosensory eyespot in the biflagellate, unicellular green algaChlamydomonas reinhardtiirequires coordinated organization of photoreceptors in the plasma membrane and pigment granule/thylakoid membrane layers in the chloroplast.min1(mini-eyed) mutant cells contain abnormally small, disorganized eyespots in which the chloroplast envelope and plasma membrane are no longer apposed. TheMIN1gene, identified here by phenotypic rescue, encodes a protein with an N-terminal C2 domain and a C-terminal LysM domain separated by a transmembrane sequence. This novel domain architecture led to the hypothesis that MIN1 is in the plasma membrane or the chloroplast envelope, where membrane association of the C2 domain promotes proper eyespot organization. Mutation of conserved C2 domain loop residues disrupted association of the MIN1 C2 domain with the chloroplast envelope in moss cells but did not abolish eyespot assembly inChlamydomonas. Inmin1null cells, channelrhodopsin-1 (ChR1) photoreceptor levels were reduced, indicating a role for MIN1 in ChR1 expression and/or stability. However, ChR1 localization was only minimally disturbed during photoautotrophic growth ofmin1cells, conditions under which the pigment granule layers are disorganized. The data are consistent with the hypothesis that neither MIN1 nor proper organization of the plastidic components of the eyespot is essential for localization of ChR1.