Cloning and Stress-Induced Expression Analysis of Calmodulin in the Antarctic Alga Chlamydomonas sp. ICE-L
Calmodulin (CaM) is a Ca 2+ -binding protein that plays a role in several Ca 2+ signaling pathways, which dynamically regulates the activities of hundreds of proteins. The ice alga Chlamydomonas sp. ICE-L, which has the ability to adapt to extreme polar conditions, is a crucial primary producer in A...
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Published in | Current microbiology Vol. 74; no. 8; pp. 921 - 929 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
New York
Springer US
01.08.2017
Springer Nature B.V |
Subjects | |
Online Access | Get full text |
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Summary: | Calmodulin (CaM) is a Ca
2+
-binding protein that plays a role in several Ca
2+
signaling pathways, which dynamically regulates the activities of hundreds of proteins. The ice alga
Chlamydomonas
sp. ICE-L, which has the ability to adapt to extreme polar conditions, is a crucial primary producer in Antarctic ecosystem. This study hypothesized that
Cam
helps the ICE-L to adapt to the fluctuating conditions in the polar environment. It first verified the overall length of
Cam
, through RT-PCR and RACE-PCR, based on partial
Cam
transcriptome library of ICE-L. Then, the nucleotide and predicted amino acid sequences were, respectively, analyzed by various bioinformatics approaches to gain more insights into the computed physicochemical properties of the CaM. Potential involvements of
Cam
in responding to certain stimuli (i.e., UVB radiation, high salinity, and temperature) were investigated by differential expression, measuring its transcription levels by means of quantitative RT-PCR. Results showed that CaM was indeed inducible and regulated by high UVB radiation, high salinity, and nonoptimal temperature conditions. Different conditions had different expression tendencies, which provided an important basis for investigating the adaptation mechanism of
Cam
in ICE-L. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0343-8651 1432-0991 |
DOI: | 10.1007/s00284-017-1263-5 |