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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
21
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pubmed:dateCreated |
2007-8-13
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pubmed:abstractText |
Human lens beta-crystallin contains four acidic (betaA1-->betaA4) and three basic (betaB1-->betaB3) subunits. They oligomerize in the lens, but it is uncertain which subunits are involved in the oligomerization. We used a two-hybrid system to detect protein-protein interactions systematically. Proteins were also expressed for some physicochemical studies. The results indicate that all acidic-basic pairs (betaA-betaB) except betaA4-betaBs pairs show strong hetero-molecular interactions. For acidic or basic pairs, only two pairs (betaA1-betaA1 and betaA3-betaA3) show strong self-association. betaA2 and betaA4 show very weak self-association, which arises from their low solubility. Confocal fluorescence microscopy shows enormous protein aggregates in betaA2- or betaA4-crystallin transfected cells. However, coexpression with betaB2-crystallin decreased both the number and size of aggregates. Circular dichroism indicates subtle differences in conformation among beta-crystallins that may have contributed to the differences in interactions.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17662718-10049695,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17662718-10366513,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17662718-10610780,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17662718-10625643,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17662718-11180977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17662718-11700327,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17662718-12957141,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17662718-14573871,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17662718-15273315,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17662718-15889016,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17662718-1595904,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17662718-16319073,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17662718-16774643,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17662718-16906755,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17662718-17615546,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17662718-2397202,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17662718-3052280,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17662718-3773734,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17662718-4063377,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17662718-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17662718-6775970,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17662718-8344494,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17662718-8345525,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17662718-9514125,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17662718-9702175,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17662718-9774426
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
581
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3936-42
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pubmed:dateRevised |
2011-9-26
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pubmed:meshHeading |
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pubmed:year |
2007
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pubmed:articleTitle |
Protein-protein interactions among human lens acidic and basic beta-crystallins.
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pubmed:affiliation |
Center for Ophthalmic Research/Surgery, Brigham and Women's Hospital, Department of Ophthalmology, Harvard Medical School, Boston, MA 02115, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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