Binding of pigments to the cyanobacterial high-light-inducible protein HliC

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F18%3A43897486" target="_blank" >RIV/60076658:12310/18:43897486 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388971:_____/18:00491694

Výsledek na webu

<a href="https://link.springer.com/content/pdf/10.1007%2Fs11120-017-0475-7.pdf" target="_blank" >https://link.springer.com/content/pdf/10.1007%2Fs11120-017-0475-7.pdf</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s11120-017-0475-7" target="_blank" >10.1007/s11120-017-0475-7</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Binding of pigments to the cyanobacterial high-light-inducible protein HliC

Popis výsledku v původním jazyce

Cyanobacteria possess a family of one-helix high-light-inducible proteins (HLIPs) that are widely viewed as ancestors of the light-harvesting antenna of plants and algae. HLIPs are essential for viability under various stress conditions, although their exact role is not fully understood. The unicellular cyanobacterium Synechocystis sp. PCC 6803 contains four HLIPs named HliA-D, and HliD has recently been isolated in a small protein complex and shown to bind chlorophyll and beta-carotene. However, no HLIP has been isolated and characterized in a pure form up to now. We have developed a protocol to purify large quantities of His-tagged HliC from an engineered Synechocystis strain. Purified His-HliC is a pigmented homo-oligomer and is associated with chlorophyll and beta-carotene with a 2:1 ratio. This differs from the 3:1 ratio reported for HliD. Comparison of these two HLIPs by resonance Raman spectroscopy revealed a similar conformation for their bound beta-carotenes, but clear differences in their chlorophylls. We present and discuss a structural model of HliC, in which a dimeric protein binds four chlorophyll molecules and two beta-carotenes.

Název v anglickém jazyce

Binding of pigments to the cyanobacterial high-light-inducible protein HliC

Popis výsledku anglicky

Cyanobacteria possess a family of one-helix high-light-inducible proteins (HLIPs) that are widely viewed as ancestors of the light-harvesting antenna of plants and algae. HLIPs are essential for viability under various stress conditions, although their exact role is not fully understood. The unicellular cyanobacterium Synechocystis sp. PCC 6803 contains four HLIPs named HliA-D, and HliD has recently been isolated in a small protein complex and shown to bind chlorophyll and beta-carotene. However, no HLIP has been isolated and characterized in a pure form up to now. We have developed a protocol to purify large quantities of His-tagged HliC from an engineered Synechocystis strain. Purified His-HliC is a pigmented homo-oligomer and is associated with chlorophyll and beta-carotene with a 2:1 ratio. This differs from the 3:1 ratio reported for HliD. Comparison of these two HLIPs by resonance Raman spectroscopy revealed a similar conformation for their bound beta-carotenes, but clear differences in their chlorophylls. We present and discuss a structural model of HliC, in which a dimeric protein binds four chlorophyll molecules and two beta-carotenes.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10606 - Microbiology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2018

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Photosynthesis Research

ISSN

0166-8595

e-ISSN

—

Svazek periodika

137

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

11

Strana od-do

29-39

Kód UT WoS článku

000435365700003

EID výsledku v databázi Scopus

2-s2.0-85039060214