2007
DOI: 10.1074/jbc.m605463200
|View full text |Cite
|
Sign up to set email alerts
|

Localization of the Small CAB-like Proteins in Photosystem II

Abstract: The cyanobacterial small CAB-like proteins (SCPs) consist of one-helix proteins that resemble transmembrane regions of the light-harvesting proteins of plants. To determine whether these proteins are associated with protein complexes in the thylakoid membrane, an abundant member of the SCP family, ScpD, was marked with a His tag, and proteins co-isolating with His-tagged ScpD were identified. These proteins included the major Photosystem (PS) II components as well as FtsH, which is involved in degradation of t… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1

Citation Types

2
71
2

Year Published

2007
2007
2017
2017

Publication Types

Select...
6
1
1

Relationship

2
6

Authors

Journals

citations
Cited by 89 publications
(76 citation statements)
references
References 59 publications
2
71
2
Order By: Relevance
“…This protein family, also called small cab-like proteins, aids in high-light survival and photoacclimation in Synechocystis (He et al, 2001;Havaux et al, 2003), and may also have a role in light-shock tolerance in eNATL. The mechanism by which they do this remains unclear, but high light-inducible proteins are thought to physically associate with either photosystem and allow it to shed excess energy as heat and thereby reduce photoinactivation (Promnares et al, 2006;Yao et al, 2007). As a photosynthetic organism, reducing and reversing the effects of photosystem inactivation is crucial for the survival of Prochlorococcus exposed to high light levels.…”
Section: Response To Light Shock In Cultured Isolatesmentioning
confidence: 99%
“…This protein family, also called small cab-like proteins, aids in high-light survival and photoacclimation in Synechocystis (He et al, 2001;Havaux et al, 2003), and may also have a role in light-shock tolerance in eNATL. The mechanism by which they do this remains unclear, but high light-inducible proteins are thought to physically associate with either photosystem and allow it to shed excess energy as heat and thereby reduce photoinactivation (Promnares et al, 2006;Yao et al, 2007). As a photosynthetic organism, reducing and reversing the effects of photosystem inactivation is crucial for the survival of Prochlorococcus exposed to high light levels.…”
Section: Response To Light Shock In Cultured Isolatesmentioning
confidence: 99%
“…7). Recent results showing the association of so-called high light-induced proteins with PSII (Promnares et al, 2006;Yao et al, 2007) and their presumable role in the temporary binding of Chl during the PSII repair-related D1 replacement (Vavilin et al, 2007) indicate that Chl molecules released from the degraded D1 can be reused. It is possible that the lack of the newly synthesized CP47 allows more Chl precursors to be utilized for the synthesis of Chl consumed during selective D1 turnover.…”
Section: Role Of Psb28 Protein In the Synthesis Of Chl And Chl-bindinmentioning
confidence: 99%
“…The Ycf39-HliD complex was recently purified from Synechocystis and, because the Ycf39 itself does not bind pigments (15), the analysis of the Ycf39-HliD complex allowed for identification of certain spectroscopic properties of the HliD protein. The results revealed that HliD binds Chl a and ␤-carotene in a conformation that dissipates energy via singlet-singlet energy transfer from the Chl a Q y state to the ␤-carotene S 1 state (19).…”
mentioning
confidence: 99%
“…They are likely to play photoprotective and regulatory functions during synthesis and degradation of chlorophyll-binding proteins and during assembly and repair of Photosystem II (14). The cyanobacterium Synechocystis PCC 6083 contains four different Hlips (HliA-HliD) and all four of these small membrane proteins bind to early intermediates of the Photosystem II assembly (15,16). Moreover, the HliD and HliC also form stable complexes with chlorophyll synthase, the terminal enzyme of Chl a biosynthesis (17,18), and with the Ycf39 protein (15,17).…”
mentioning
confidence: 99%
See 1 more Smart Citation