TURNING THE TIDE ON MARINE MANAGEMENT
Thursday, 25 June 2015: Media Release
The NSW Government is improving the management of our precious marine estate with the launch of a new Threat and Risk Assessment Framework.
Minister for Primary Industries, Niall Blair, and Minister for the Environment, Mark Speakman, today released new guidelines on how the NSW Government will assess the threats and risks to our marine estate.
“Last year, an historic bill passed the NSW Parliament to make sure the state’s marine estate is managed based on science and not politics,” Mr Blair said.
“This is the first step in implementing this Marine Estate Management Act 2014, which sets out a robust legal requirement to assess economic, social and environmental threats, such as pollution, loss of biodiversity, restricted access, anti-social behaviour, and impacts of pests and diseases.
“This framework, developed by the Marine Estate Management Authority with expert guidance from the Marine Estate Expert Knowledge Panel, is at the heart of the NSW Liberals & Nationals Government’s new era in marine estate management.”
Mr Speakman said the framework will consider not only the imminent threats to our coasts and marine waters, but also the cumulative impacts and potential threats over the coming decades.
“This will allow the NSW Government to focus its efforts around the key threats to the marine environment, and deliver on its vision for a healthy coast and sea,” Mr Speakman said.
“We are committed to managing our marine environment for the greatest well-being of the community, now and into the future.”
Initially the framework will be applied to two key projects:
- a state-wide Marine Estate Threat and Risk Assessment; and
- the Hawkesbury Shelf Marine Bioregion Assessment, covering the area from Newcastle to Shellharbour.
The community is encouraged to have their say about both of these projects and the framework in the coming months, and the Authority may refine the framework over time after it has been applied to the first two projects.
The Ministers also today launched an interactive web portal to allow the community to have input into the Hawkesbury Shelf Marine Bioregion Assessment by providing local information on benefits and threats associated with their favourite sites within the bioregion.
The NSW Government is now seeking crucial information from the public regarding sites within the bioregion, the benefits they gain from their use of these sites, and what they see as key threats and ideas on how to manage those threats.
Along with expert input, the information people provide will help identify management options to enhance marine biodiversity conservation whilst maximising community benefits.”
Eleven sites in the Hawkesbury marine bioregion have already been identified for priority assessment and the community is invited to nominate additional sites via the web portal that they would like to see considered:
• Barrenjoey Head (an existing Aquatic Reserve)
• Bouddi National Park Marine Extension
• Bronte-Coogee (an existing Aquatic Reserve)
• Cape Banks (an existing Aquatic Reserve)
• Chowder Bay
• Long Reef (an existing Aquatic Reserve)
• Narrabeen Head (an existing Aquatic Reserve)
• North Harbour (an existing Aquatic Reserve)
• North Harbour extension – Manly Wharf and Manly Cove
• Magic Point, Malabar
• Wybung Head
The web portal, framework and more information can be accessed at www.marine.nsw.gov.au
Direct Link to page: www.marine.nsw.gov.au/key-initiatives/hawkesbury-shelf-marine-assessment/hawkesbury-shelf-marine-bioregion-assessment-webportal
The web portal will be open until 28 August 2015.
National Tree Day 2015
26th Jul 2015: 9am - 9am
Come along to Whitney Reserve, Pittwater’s venue to participate in this year's National Tree Day. Come along and help plant areas of the creekline and adjacent slope with native plants.
Please wear appropriate clothing (long sleeves, trousers, sturdy shoes and a hat) and bring a bottle of water.
Council will provide you with refreshments and free native plants for you to plant in your own garden.
Venue: Whitney Reserve, Whitney Street, Mona Vale
Contact: Jenny Cronan at Pittwater Council - 9970 1357
Website: treeday.planetark.org/site/10008760
Australians forced to wait 15 months for new drugs vs US & Europe: Report
Lord of the Rings – distance to bizarre galactic X-ray source determined
24 JUN 2015: DEBORAH SMITH UNSW
Astronomers have measured the distance to one of the Milky Way’s most bizarre objects for the first time, using the Australian Mopra radio telescope near Coonabarabran.
Rings in X-ray light surrounding the bizarre X-ray binary star Circinus X-1. Image NASA/CXC/Univ. of Wisconsin-Madison/S.Heinz et al; Optical: DSS
Astronomers have measured the distance to one of the Milky Way’s most bizarre objects for the first time, using the Australian Mopra radio telescope near Coonabarabran.
Circinus X-1 is a binary star system that exploded a mere 2,500 years ago. It consists of a dense, collapsed neutron star, still in the orbital embrace of its companion star, and flashes X-rays as material from the companion star spirals into the neutron star and reaches high temperatures.
“We have been able to work out that this strange object is 31,000 light years away, using Mopra’s ability to detect clouds of dust in interstellar space,” says study co-author, UNSW astrophysicist, Professor Michael Burton.
UNSW’s Dr Catherine Braiding, also a study co-author, adds: "Circinus X-1 acts in some ways like a neutron star and in some like a black hole. It's extremely unusual to find an object that has such a blend of these properties."
The research will be published in the Astrophysical Journal and is available now online.
In late 2013, Circinus-X gave off a massive burst of X-rays in an event that lasted about two months. The flare was monitored by a detector on board the International Space Station.
Researchers led by Professor Sebastian Heinz at the University of Wisconsin-Madison then quickly mounted a series of follow-up observations using two space-based telescopes – the Chandra X-ray Observatory and the XMM-Newton Observatory.
They discovered four bright rings of X-rays around the neutron star at the heart of Circinus X-1.
“These rings indicated there were dense clouds of gas between us and Circinus X-1, and that some of the X-rays from the massive outburst had been deflected off these particles of dust on their way to Earth,” says Professor Burton.
“Using Mopra, we were able to find these clouds of gas, and locate their distance from us.
"We like to call this system the 'Lord of the Rings', but this one has nothing to do with Sauron. The beautiful match between the Chandra X-ray rings and the Mopra radio images of the different clouds is really a first in astronomy."
The team then worked out the distance to Circinus X-1, based on the differences in time it took X-rays to reach Earth directly and to reach Earth on a longer trajectory after being deflected by the gas clouds.
“Distance measurements in astronomy are difficult, especially to sources like Circinus X-1, which are hidden in the plane of the galaxy behind a thick layer of dust, which basically makes it impossible to observe them with optical telescopes,” says Professor Heinz.
“In this case we used the dust that otherwise gets in the way to pioneer a new method for estimating distance to X-ray sources.”
The Mopra Telescope is a 22-metre single-dish radio telescope near Coonabarabran, 450 kilometres from Sydney. It has been mapping the centre of our galaxy, the Milky Way, for more than four years but is due to close later this year due to Federal Government funding cuts.
Earth's daily rotation period encoded in an atomic-level protein structure
June 25, 2015 - A collaborative group of Japanese researchers has demonstrated that the Earth's daily rotation period (24 hours) is encoded in the KaiC protein at the atomic level, a small, 10 nm-diameter biomolecule expressed in cyanobacterial cells.
This research group included: Dr. Jun Abe, Assistant Prof. Atsushi Mukaiyama, and Prof. Shuji Akiyama of the Institute for Molecular Science (IMS) Research Center of Integrative Molecular Systems (CIMoS); Assistant Prof. Toshifumi Mori and Prof. Shinji Saito of the Department of Theoretical and Computational Molecular Science at IMS; Designated Prof. Takao Kondo of Nagoya University; and Assistant Prof. Eiki Yamashita of the Osaka University Institute for Protein Research.
The results of this joint research will help elucidate a longstanding question in chronobiology: How is the circadian period of biological clocks determined? The results will also help understand the basic molecular mechanism of the biological clock. This knowledge might contribute to the development of therapies for disorders associated with abnormal circadian rhythms.
In accordance with diurnal changes in the environment (notably light intensity and temperature) resulting from the Earth's daily rotation around its axis, many organisms regulate their biological activities to ensure optimal fitness and efficiency. The biological clock refers to the mechanism whereby organisms adjust the timing of their biological activities. The period of this clock is set to approximately 24 hours. A wide range of studies have investigated the biological clock in organisms ranging from bacteria to mammals. Consequently, the relationship between the biological clock and multiple diseases has been clarified. However, it remains unclear how 24-hour circadian rhythms are implemented.
The research group mentioned above addressed this question using cyanobacteria. The cyanobacterial circadian clock can be reconstructed by mixing three clock proteins (KaiA, KaiB, and KaiC) and ATP. A study published in 2007 showed that KaiC ATPase activity, which mediates the ATP hydrolysis reaction, is strongly associated with circadian periodicity. The results of that study indicated that the functional structure of KaiC could be responsible for determining the circadian rhythm.
KaiC ATPase activity exhibits a robust circadian oscillation in the presence of KaiA and KaiB proteins. In the study reported here, the temporal profile of KaiC ATPase activity exhibited an attenuating and oscillating component even in the absence of KaiA and KaiB. A close analysis revealed that this signal had a frequency of 0.91 day-1, which approximately coincided with the 24-hour period. Thus, KaiC is the source of a steady cycle that is in tune with the Earth's daily rotation.
To identify causal structural factors, the N-terminal domain of KaiC was analyzed using high-resolution crystallography. The resultant atomic structures revealed the underlying cause of KaiC's slowness relative to other ATPases. "A water molecule is prevented from attacking into the ideal position for the ATP hydrolysis by a steric hindrance near ATP phosphoryl groups. In addition, this hindrance is surely anchored to a spring-like structure derived from polypeptide isomerization," elaborates Dr. Jun Abe. "The ATP hydrolysis, which involves access of a water molecule to the bound ATP and reverse isomerization of the polypeptide, is expected to require a significantly larger amount of free energy than for typical ATP hydrolysis. Thus, the three-dimensional atomic structure discovered in this study explains why the ATPase activity of KaiC is so much lower (by 100- to 1,000,000-fold) than that of typical ATPase molecules."
The circadian clock's period is independent of ambient temperature, a phenomenon known as temperature compensation. One KaiC molecule is composed of six identical subunits, each containing duplicated domains with a series of ATPase motifs. The asymmetric atomic-scale regulation by the aforementioned mechanism dictates a feedback mechanism that maintains the ATPase activity at a constant low level. The authors of this study discovered that the Earth's daily rotation period (24 hours) is implemented as the time constant of the feedback mechanism mediated in this protein structure.
Technological Implications
KaiC and other protein molecules are capable of moving on short time scales, on the order of 10-12 to 10-1 seconds. This study provides the first atomic-level demonstration that small protein molecules can generate 24-hour rhythms by regulating molecular structure and reactivity. Lab head and CIMoS Director Porf. Shuji Akiyama sees, "The fact that a water molecule, ATP, the polypeptide chain, and other universal biological components are involved in this regulation suggests that humans and other complex organisms may also share a similar molecular machinery. In the crowded intracellular environment that contains a myriad of molecular signals, KaiC demonstrates long-paced oscillations using a small amount of energy generated through ATP consumption. This clever mechanism for timekeeping in a noisy environment may inspire development of highly efficient and sustainable chemical reaction processes and molecular-system-based information processing."
Glossary
1) Clock protein: A clock protein plays an essential role in the circadian pacemaker. Mutations and deficiencies in clock proteins can alter the intrinsic characteristics of circadian rhythm.
2) ATP: Adenosine triphosphate is a source of energy required for muscle contraction and many other biological activities. ATP, a nucleotide that mediates the storage and consumption of energy, is sometimes referred to as the "currency of biological energy" due to its universality and importance in metabolism. ATP consists of an adenosine molecule bound to three phosphate groups. Upon hydrolysis, the ATPase releases one phosphate molecule plus approximately 8 kcal/mol of energy.
3) Polypeptide isomerization: Protein polypeptide main chains undergo isomerization on a time scale of seconds or longer; therefore, protein isomerization is one of the slowest biological reactions. Most functional protein main chains have a trans conformation, and a few proteins have a functional cis conformation.
Jun Abe, Takuya B. Hiyama, Atsushi Mukaiyama, Seyoung Son, Toshifumi Mori, Shinji Saito, Masato Osako, Julie Wolanin, Eiki Yamashita, Takao Kondo, and Shuji Akiyama. Atomic-scale origins of slowness in the cyanobacterial circadian clock. Science, 25 June 2015 DOI: 10.1126/science.1261040
